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UniProtKB - V5YM14 (DAPB2_PSEMX)

Entry version 27 (02 Jun 2021)
Sequence version 1 (19 Feb 2014)
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Protein

Dipeptidyl aminopeptidase BII

Gene

dapb2

Organism
Pseudoxanthomonas mexicana
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Exopeptidase that catalyzes the removal of dipeptide units (NH2-P2-P1-) from the free amino termini of oligopeptides and small proteins (PubMed:24598890, PubMed:8892831, PubMed:24827749).

Peptide digestion is sequential and substrate recognition is non-specific, with the exception that Pro is not suitable as a P1 residue (PubMed:24827749).

Removes many residues of bioactive oligopeptides such as angiotensin I and neuromedin N and cleaves also oxidized insulin B chain. Able to hydrolyze an X-Pro bond, an imido bond. No endopeptidase activity (PubMed:8892831).

May play a physiological role in feeding (PubMed:24598890).

3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Completely inhibited by the serine protease inhibitor diisopropyl fluorophosphate (DFP) and potently inhibited by 0.5 mM ZnCl2, 10 mM o-phenanthlorine, phenylmethanesulfonyl fluoride (PMSF) and N-tosyl-L-phenyl-alanyl chloromethyl ketone (TPCK), but not by N-tosyl-L-lysyl chloromethyl ketone (TLCK). Activity is not affected significantly by protease inhibitors, such as chymostatin, leupeptin, N-ethylmaleimide (NEM), iodoacetate (IAA), L-trans-epoxysuccinyl-leucylamido(4-guanido)butane (E64) and pepstatin A or by CoCl2, CaCl2 and EDTA.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=1.7 mM for Gly-Phe-pNA (at pH 8 and 37 degrees Celsius)1 Publication
  2. KM=0.87 mM for Ala-Ala-pNA (at pH 8 and 37 degrees Celsius)1 Publication
  3. KM=7.2 mM for Gly-Phe-beta-naphthylamine (at pH 8 and 37 degrees Celsius)1 Publication
  1. Vmax=3.4 µmol/min/mg enzyme with Gly-Phe-pNA as substrate2 Publications
  2. Vmax=10 µmol/min/mg enzyme with Ala-Ala-pNA as substrate2 Publications
  3. Vmax=9.4 µmol/min/mg enzyme with Gly-Phe-pNA as substrate (at pH 8 and 37 degrees Celsius)1 Publication
  4. Vmax=20 µmol/min/mg enzyme with Ala-Ala-pNA as substrate (at pH 8 and 37 degrees Celsius)1 Publication
  5. Vmax=10 µmol/min/mg enzyme with Gly-Phe-beta-naphthylamine as substrate (at pH 8 and 37 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 8 for the hydrolysis of Gly-Phe-pNA.1 Publication

Temperature dependencei

Optimum temperature is approximately 30 degrees Celsius for the hydrolysis of Gly-Phe-pNA. Stable at a temperature below 20 degrees Celsius for 30 minutes.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei86Charge relay system2 Publications1
Active sitei224Charge relay system2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei330Substrate1 Publication1
Active sitei657Charge relay system2 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAminopeptidase, Hydrolase, Protease

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.4.11.6, 14090

Protein family/group databases

MEROPS protease database

More...MEROPSi		S46.003

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Dipeptidyl aminopeptidase BIIImported (EC:3.4.14.-4 Publications)
Short name:
DAP BII2 Publications
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:dapb2Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiPseudoxanthomonas mexicana
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri128785 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Pseudoxanthomonas

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Designing engineered forms of this protein with the ability to produce custom dipeptides potentially may have a number of commercial and industrial uses including food industry (PubMed:8892831, PubMed:24827749). Maybe useful for drug design (PubMed:24827749).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi86H → A: Loss of enzymatic activity. Loss of enzymatic activity; when associated with A-224 and A-657. 2 Publications1
Mutagenesisi195D → A: Decreased enzymatic activity to 23 percent relative to wild-type. 1 Publication1
Mutagenesisi214D → A: Decreased enzymatic activity to 1.5 percent relative to wild-type. 1 Publication1
Mutagenesisi214D → N: Decreased enzymatic activity to 3.0 percent relative to wild-type. 1 Publication1
Mutagenesisi215N → A: Loss of enzymatic activity. 1 Publication1
Mutagenesisi216W → A: Loss of enzymatic activity. 1 Publication1
Mutagenesisi224D → A: Decreased enzymatic activity to 0.026 percent relative to wild-type. Loss of enzymatic activity; when associated with A-86 and A-657. 2 Publications1
Mutagenesisi224D → N: Decreased enzymatic activity to 0.15 percent relative to wild-type. 1 Publication1
Mutagenesisi330N → A: Loss of enzymatic activity. 1 Publication1
Mutagenesisi522D → A: Decreased enzymatic activity to 32 percent relative to wild-type. 1 Publication1
Mutagenesisi522D → N: Decreased enzymatic activity to 16 percent relative to wild-type. 1 Publication1
Mutagenesisi574D → A: Decreased enzymatic activity to 83 percent relative to wild-type. 1 Publication1
Mutagenesisi574D → N: Decreased enzymatic activity to 21 percent relative to wild-type. 1 Publication1
Mutagenesisi657S → A: Loss of enzymatic activity. Loss of enzymatic activity; when associated with A-86 and A-224. 2 Publications1
Mutagenesisi674D → A: Loss of enzymatic activity. 1 Publication1
Mutagenesisi675G → R: Acquires the enzymatic activity for synthetic substrates with Asp/Glu at P1 position. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 241 PublicationAdd BLAST24
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000043346325 – 722Dipeptidyl aminopeptidase BIISequence analysisAdd BLAST698

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi70 ↔ 87Combined sources1 Publication
Disulfide bondi166 ↔ 174Combined sources1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		V5YM14

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

2 Publications

GO - Molecular functioni

Complete GO annotation on QuickGO ...

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1722
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		V5YM14

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni215 – 216Substrate-binding1 Publication2
Regioni655 – 657Substrate-binding1 Publication3
Regioni673 – 674Substrate-binding1 Publication2

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The chymotrypsin fold (25-276 and 574-722) is the catalytic domain and the alpha-helical domain (277-573) is the regulatory domain necessary for exopeptidase activity.1 Publication

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase S46 family.2 Publications

Keywords - Domaini

Signal

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.40.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR019500, Pep_S46
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin

The PANTHER Classification System

More...PANTHERi		PTHR38469, PTHR38469, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF10459, Peptidase_S46, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50494, SSF50494, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

V5YM14-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRPNLLAAAI AVPLSLLAAQ IAQAGEGMWV PQQLPEIAGP LKKAGLKLSP 
        60         70         80         90        100
QQISDLTGDP MGAVVALGGC TASFVSPNGL VVTNHHCAYG AIQLNSTAEN 
       110        120        130        140        150
NLIKNGFNAP TTADEVSAGP NARVFVLDEI TDVTKDAKAA IAAAGDDALA 
       160        170        180        190        200
RTKALEAFEK KLIADCEAEA GFRCRLYSFS GGNTYRLFKN LEIKDVRLAY 
       210        220        230        240        250
APPGSVGKFG GDIDNWMWPR HTGDFAFYRA YVGKDGKPAA FSKDNVPYQP 
       260        270        280        290        300
KHWLKFADQP LGAGDFVMVA GYPGSTNRYA LAAEFDNTAQ WTYPTIARHY 
       310        320        330        340        350
KNQIAMVEAA GKQNADIQVK YAATMAGWNN TSKNYDGQLE GFKRIDAAGQ 
       360        370        380        390        400
KLREEAAVLG WLKGQGAKGQ PALDAHAKLL DLLEQSKATR DRDLTLALFN 
       410        420        430        440        450
NTAMLGSATQ LYRLSIEREK PNAERESGYQ ERDLPAIEGG LKQLERRYVA 
       460        470        480        490        500
AMDRQLQEYW LNEYIKLPAD QRVAAVDAWL GGNDAAAVKR ALDRLAGTKL 
       510        520        530        540        550
GSTEERLKWF AADRKAFEAS NDPAIQYAVA VMPTLLKLEQ ERKTRAGENL 
       560        570        580        590        600
AARPVYLQAL ADYKKSQGEF VYPDANLSLR ITFGNVMGYA PKDGMEYTPF 
       610        620        630        640        650
TTLEGVVAKE TGQDPFDSPK ALLDAVAAKR YGGLEDKRIG SVPVNYLSDL 
       660        670        680        690        700
DITGGNSGSP VLDAHGKLVG LAFDGNWESV SSNWVFDPKM TRMIAVDGRY 
       710        720 
LRWIMQEVYP APQLLKEMNV GK
Length:722
Mass (Da):78,698
Last modified:February 19, 2014 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i5CD59AD3A975C760
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AB889525 Genomic DNA Translation: BAO18427.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB889525 Genomic DNA Translation: BAO18427.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3WOIX-ray2.10A/B25-722[»]
3WOJX-ray2.20A/B25-722[»]
3WOKX-ray1.95A/B25-722[»]
3WOLX-ray1.74A/B25-722[»]
3WOMX-ray1.86A/B25-722[»]
3WONX-ray1.75A/B25-722[»]
3WOOX-ray1.80A/B25-722[»]
3WOPX-ray1.95A/B25-722[»]
3WOQX-ray1.82A/B25-722[»]
3WORX-ray2.10A/B25-722[»]
4Y06X-ray2.18A/B1-722[»]
SMRiV5YM14
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

MEROPSiS46.003

Proteomic databases

PRIDEiV5YM14

Enzyme and pathway databases

BRENDAi3.4.11.6, 14090

Family and domain databases

Gene3Di2.40.10.10, 1 hit
InterProiView protein in InterPro
IPR019500, Pep_S46
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
PANTHERiPTHR38469, PTHR38469, 1 hit
PfamiView protein in Pfam
PF10459, Peptidase_S46, 1 hit
SUPFAMiSSF50494, SSF50494, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDAPB2_PSEMX
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: V5YM14
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 24, 2015
Last sequence update: February 19, 2014
Last modified: June 2, 2021
This is version 27 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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