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Protein
Submitted name:

Lectin

Gene
N/A
Organism
Pterocarpus angolensis (Kiaat tree) (Bleedwood tree)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531MannoseCombined sources
Binding sitei91 – 911Beta-D-mannoseCombined sources
Binding sitei94 – 941GlucoseCombined sources
Binding sitei114 – 1141Glucose; via amide nitrogenCombined sources
Metal bindingi136 – 1361Calcium 1Combined sources
Metal bindingi136 – 1361ManganeseCombined sources
Metal bindingi138 – 1381Calcium 1Combined sources
Metal bindingi138 – 1381Calcium 2Combined sources
Metal bindingi138 – 1381ManganeseCombined sources
Metal bindingi140 – 1401Calcium 2; via carbonyl oxygenCombined sources
Binding sitei140 – 1401GlucoseCombined sources
Binding sitei140 – 1401MannoseCombined sources
Metal bindingi146 – 1461Calcium 2Combined sources
Binding sitei146 – 1461GlucoseCombined sources
Metal bindingi149 – 1491Calcium 1Combined sources
Metal bindingi149 – 1491Calcium 2Combined sources
Metal bindingi149 – 1491ManganeseCombined sources
Metal bindingi154 – 1541Calcium 1; via tele nitrogenCombined sources
Metal bindingi154 – 1541Manganese; via tele nitrogenCombined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

CalciumCombined sources, LectinSAAS annotation, ManganeseCombined sources, Metal-bindingCombined sources

Names & Taxonomyi

Protein namesi
Submitted name:
LectinImported
OrganismiPterocarpus angolensis (Kiaat tree) (Bleedwood tree)Imported
Taxonomic identifieri182271 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeDalbergieaePterocarpus

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91Pyrrolidone carboxylic acidCombined sources
Glycosylationi126 – 1261N-linked (GlcNAc...)Combined sourcesCAR_5006759698

Keywords - PTMi

Pyrrolidone carboxylic acidCombined sources

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N3OX-ray2.00A/B9-260[»]
1N3PX-ray2.10A/B9-260[»]
1N3QX-ray2.20A/B9-260[»]
1Q8OX-ray2.20A/B10-260[»]
1Q8PX-ray1.75A/B10-260[»]
1Q8QX-ray2.05A/B10-260[»]
1Q8SX-ray2.05A/B10-260[»]
1Q8VX-ray1.85A/B10-260[»]
1S1AX-ray1.80A/B9-260[»]
1UKGX-ray1.70A/B9-260[»]
2AR6X-ray1.80A/B9-260[»]
2ARBX-ray1.80A/B9-260[»]
2AREX-ray1.80A/B9-260[»]
2ARXX-ray2.00A/B9-260[»]
2AUYX-ray1.95A/B9-260[»]
2GMEX-ray1.75A/B9-260[»]
2GMMX-ray2.15A/B10-260[»]
2GMPX-ray2.50A/B9-260[»]
2GN3X-ray1.97A/B9-260[»]
2GN7X-ray2.90A/B9-260[»]
2GNBX-ray2.27A/B9-260[»]
2GNDX-ray2.25A/B9-260[»]
2GNMX-ray1.95A/B9-260[»]
2GNTX-ray2.02A/B9-260[»]
2PHFX-ray2.10A/B9-260[»]
2PHRX-ray1.90A/B9-260[»]
2PHTX-ray2.10A/B9-260[»]
2PHUX-ray2.20A/B9-260[»]
2PHWX-ray1.80A/B9-260[»]
2PHXX-ray1.80A/B9-260[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 250240Lectin_legBInterPro annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni91 – 944Mannose bindingCombined sources
Regioni113 – 1142Mannose bindingCombined sources
Regioni144 – 1463Mannose bindingCombined sources
Regioni144 – 1452Beta-D-mannose bindingCombined sources
Regioni144 – 1452Fructose bindingCombined sources
Regioni228 – 2303Glucose bindingCombined sources
Regioni228 – 2303Mannose bindingCombined sources
Regioni229 – 2302Beta-D-mannose bindingCombined sources
Regioni229 – 2302Fructose bindingCombined sources

Sequence similaritiesi

Belongs to the leguminous lectin family.SAAS annotation

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR016363. Lectin.
IPR000985. Lectin_LegA_CS.
IPR019825. Lectin_legB_Mn/Ca_BS.
IPR001220. Legume_lectin_dom.
[Graphical view]
PfamiPF00139. Lectin_legB. 1 hit.
[Graphical view]
PIRSFiPIRSF002690. L-type_lectin_plant. 1 hit.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00308. LECTIN_LEGUME_ALPHA. 1 hit.
PS00307. LECTIN_LEGUME_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8GSD2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLNKAYSQD SLSFGFPTFP SDQKNLIFQG DAQIKNNAVQ LTKTDSNGNP
60 70 80 90 100
VASTVGRILF SAQVHLWEKS SSRVANFQSQ FSFSLKSPLS NGADGIAFFI
110 120 130 140 150
APPDTTIPSG SGGGLLGLFA PGTAQNTSAN QVIAVEFDTF YAQDSNTWDP
160 170 180 190 200
NYPHIGIDVN SIRSVKTVKW DRRDGQSLNV LVTFNPSTRN LDVVATYSDG
210 220 230 240 250
TRYEVSYEVD VRSVLPEWVR VGFSAASGEQ YQTHTLESWS FTSTLLYTAQ
260
KKGENLALEM
Length:260
Mass (Da):28,476
Last modified:March 1, 2003 - v1
Checksum:i3674D91870CE161A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11Imported

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ426056 mRNA. Translation: CAD19805.1.
AJ426061 mRNA. Translation: CAD19810.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ426056 mRNA. Translation: CAD19805.1.
AJ426061 mRNA. Translation: CAD19810.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N3OX-ray2.00A/B9-260[»]
1N3PX-ray2.10A/B9-260[»]
1N3QX-ray2.20A/B9-260[»]
1Q8OX-ray2.20A/B10-260[»]
1Q8PX-ray1.75A/B10-260[»]
1Q8QX-ray2.05A/B10-260[»]
1Q8SX-ray2.05A/B10-260[»]
1Q8VX-ray1.85A/B10-260[»]
1S1AX-ray1.80A/B9-260[»]
1UKGX-ray1.70A/B9-260[»]
2AR6X-ray1.80A/B9-260[»]
2ARBX-ray1.80A/B9-260[»]
2AREX-ray1.80A/B9-260[»]
2ARXX-ray2.00A/B9-260[»]
2AUYX-ray1.95A/B9-260[»]
2GMEX-ray1.75A/B9-260[»]
2GMMX-ray2.15A/B10-260[»]
2GMPX-ray2.50A/B9-260[»]
2GN3X-ray1.97A/B9-260[»]
2GN7X-ray2.90A/B9-260[»]
2GNBX-ray2.27A/B9-260[»]
2GNDX-ray2.25A/B9-260[»]
2GNMX-ray1.95A/B9-260[»]
2GNTX-ray2.02A/B9-260[»]
2PHFX-ray2.10A/B9-260[»]
2PHRX-ray1.90A/B9-260[»]
2PHTX-ray2.10A/B9-260[»]
2PHUX-ray2.20A/B9-260[»]
2PHWX-ray1.80A/B9-260[»]
2PHXX-ray1.80A/B9-260[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR016363. Lectin.
IPR000985. Lectin_LegA_CS.
IPR019825. Lectin_legB_Mn/Ca_BS.
IPR001220. Legume_lectin_dom.
[Graphical view]
PfamiPF00139. Lectin_legB. 1 hit.
[Graphical view]
PIRSFiPIRSF002690. L-type_lectin_plant. 1 hit.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00308. LECTIN_LEGUME_ALPHA. 1 hit.
PS00307. LECTIN_LEGUME_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Purification, characterization and amino acid sequence of the seed lectin from Pterocarpus angolensis."
    Beeckmans S., De Greve H., Read J.S., Bourjolly A., Maramba E.F., Ncube I., Deboeck F., Bouckaert J., Van Driessche E.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Crystal structure of Pterocarpus angolensis lectin in complex with glucose, sucrose, and turanose."
    Loris R., Imberty A., Beeckmans S., Van Driessche E., Read J.S., Bouckaert J., De Greve H., Buts L., Wyns L.
    J. Biol. Chem. 278:16297-16303(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 9-260 IN COMPLEX WITH CALCIUM; FRUCTOSE; GLUCOSE AND MANGANESE.
  3. "Structural basis of oligomannose recognition by the Pterocarpus angolensis seed lectin."
    Loris R., Van Walle I., De Greve H., Beeckmans S., Deboeck F., Wyns L., Bouckaert J.
    J. Mol. Biol. 335:1227-1240(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 9-260 IN COMPLEX WITH CALCIUM; MANGANESE AND MANNOSE, PYRROLIDONE CARBOXYLIC ACID AT GLN-9.
  4. "Pterocarpus angolensis seed lectin (PAL) with one binding site free and one binding site containing the disaccharide Man(a1-3)ManMe."
    Buts L., Imberty A., Wyns L., Beeckmans S., Loris R.
    Submitted (JAN-2004) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 9-260 IN COMPLEX WITH CALCIUM; MANGANESE AND MANNOSE.
  5. "Structural basis for the recognition of complex-type biantennary oligosaccharides by Pterocarpus angolensis lectin."
    Buts L., Garcia-Pino A., Imberty A., Amiot N., Boons G.J., Beeckmans S., Versees W., Wyns L., Loris R.
    FEBS J. 273:2407-2420(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 9-260 IN COMPLEX WITH BETA-D-MANNOSE; CALCIUM; MANGANESE AND MANNOSE, PYRROLIDONE CARBOXYLIC ACID AT GLN-9, GLYCOSYLATION AT ASN-126.
  6. "Interplay between metal binding and cis/trans isomerization in legume lectins: structural and thermodynamic study of P. angolensis lectin."
    Garcia-Pino A., Buts L., Wyns L., Loris R.
    J. Mol. Biol. 361:153-167(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 9-260 IN COMPLEX WITH BETA-D-MANNOSE; CALCIUM; MANGANESE AND MANNOSE, PYRROLIDONE CARBOXYLIC ACID AT GLN-9.
  7. "How a plant lectin recognizes high mannose oligosaccharides."
    Garcia-Pino A., Buts L., Wyns L., Imberty A., Loris R.
    Plant Physiol. 144:1733-1741(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 9-260 IN COMPLEX WITH BETA-D-MANNOSE; CALCIUM; MANGANESE AND MANNOSE, PYRROLIDONE CARBOXYLIC ACID AT GLN-9.

Entry informationi

Entry nameiQ8GSD2_PTEAG
AccessioniPrimary (citable) accession number: Q8GSD2
Entry historyi
Integrated into UniProtKB/TrEMBL: March 1, 2003
Last sequence update: March 1, 2003
Last modified: May 11, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.