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P15042

- DNLJ_ECOLI

UniProt

P15042 - DNLJ_ECOLI

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Protein

DNA ligase

Gene

ligA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.

Catalytic activityi

NAD+ + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + beta-nicotinamide D-ribonucleotide + (deoxyribonucleotide)(n+m).1 Publication

Cofactori

Magnesium.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei113 – 1131NAD
Active sitei115 – 1151N6-AMP-lysine intermediate1 Publication
Binding sitei136 – 1361NAD
Binding sitei173 – 1731NADBy similarity
Binding sitei290 – 2901NAD
Binding sitei314 – 3141NADCurated
Metal bindingi408 – 4081Zinc
Metal bindingi411 – 4111Zinc
Metal bindingi426 – 4261Zinc
Metal bindingi432 – 4321Zinc
Sitei487 – 4871Interaction with target DNA
Sitei492 – 4921Interaction with target DNA

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi32 – 365NADCurated
Nucleotide bindingi81 – 822NAD

GO - Molecular functioni

  1. DNA binding Source: EcoCyc
  2. DNA ligase (NAD+) activity Source: EcoCyc
  3. metal ion binding Source: UniProtKB-KW
  4. NAD+ binding Source: EcoCyc

GO - Biological processi

  1. base-excision repair, DNA ligation Source: EcoCyc
  2. DNA ligation Source: EcoCyc
  3. DNA replication Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

DNA damage, DNA repair, DNA replication

Keywords - Ligandi

Magnesium, Metal-binding, NAD, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:EG10534-MONOMER.
ECOL316407:JW2403-MONOMER.
MetaCyc:EG10534-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA ligase (EC:6.5.1.2)
Alternative name(s):
Polydeoxyribonucleotide synthase [NAD(+)]
Gene namesi
Name:ligA
Synonyms:dnaL, lig, lop, pdeC
Ordered Locus Names:b2411, JW2403
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10534. ligA.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi10 – 101E → A: No effect. 1 Publication
Mutagenesisi22 – 221Y → A or S: Reduces nick joining activity by 99.9%. 1 Publication
Mutagenesisi22 – 221Y → F: Reduces nick joining activity by 91%. 1 Publication
Mutagenesisi23 – 231H → A or Y: Reduces nick joining activity by 90%. 1 Publication
Mutagenesisi32 – 321D → A or E: Reduces nick joining activity by 99%. 1 Publication
Mutagenesisi32 – 321D → N: Reduces nick joining activity by 91%. 1 Publication
Mutagenesisi35 – 351Y → A: Reduces nick joining activity by 98%. 1 Publication
Mutagenesisi35 – 351Y → F: Reduces nick joining activity by 77%. 1 Publication
Mutagenesisi35 – 351Y → S: Reduces nick joining activity by 99.9%. 1 Publication
Mutagenesisi36 – 361D → A: Reduces nick joining activity by 99.8%. 1 Publication
Mutagenesisi36 – 361D → E: Reduces nick joining activity by 96%. 1 Publication
Mutagenesisi36 – 361D → N: Reduces nick joining activity by 88%. 1 Publication
Mutagenesisi115 – 1151K → Q or R: Reduces nick joining activity by 99.9%. 1 Publication
Mutagenesisi117 – 1171D → E: Reduces nick joining activity by 97%. 1 Publication
Mutagenesisi117 – 1171D → N: Reduces nick joining activity by 99.9%. 1 Publication
Mutagenesisi118 – 1181G → A: Reduces nick joining activity by 99.9%. 1 Publication
Mutagenesisi138 – 1381D → A: Reduces nick joining activity by 63%. 1 Publication
Mutagenesisi143 – 1431E → A: Reduces nick joining activity by 48%. 1 Publication
Mutagenesisi172 – 1721G → A: Reduces nick joining activity by 64%. 1 Publication
Mutagenesisi173 – 1731E → A, D or Q: Reduces nick joining activity by 99.9%. 1 Publication
Mutagenesisi198 – 1981N → A: Reduces nick joining activity by 74%. 1 Publication
Mutagenesisi200 – 2001R → A, K or Q: Reduces nick joining activity by 99.9%. 1 Publication
Mutagenesisi208 – 2081R → A, K or Q: Reduces nick joining activity by 99%. 1 Publication
Mutagenesisi277 – 2771R → A: Reduces nick joining activity by 99%. 1 Publication
Mutagenesisi285 – 2851D → E: Reduces nick joining activity by 96%. 1 Publication
Mutagenesisi285 – 2851D → N: Reduces nick joining activity by 99%. 1 Publication
Mutagenesisi286 – 2861G → A: Reduces nick joining activity by 86%. 1 Publication
Mutagenesisi288 – 2881V → A: Reduces nick joining activity by 25%. 1 Publication
Mutagenesisi290 – 2901K → A: Reduces nick joining activity by 87%. 1 Publication
Mutagenesisi314 – 3141K → Q: Reduces nick joining activity by 99%. 1 Publication
Mutagenesisi314 – 3141K → R: Reduces nick joining activity by 95%. 1 Publication
Mutagenesisi333 – 3331R → A or Q: Reduces nick joining activity by over 95%. Abolishes nick joining activity; when associated with A-334. 1 Publication
Mutagenesisi334 – 3341T → A: Abolishes nick joining activity; when associated with A-333. 1 Publication
Mutagenesisi342 – 3421R → A: Reduces nick joining activity by 80%. 1 Publication
Mutagenesisi379 – 3791R → A or Q: Reduces nick joining activity by over 95%. 1 Publication
Mutagenesisi383 – 3842VI → AA: Reduces nick joining activity by 95%. 1 Publication
Mutagenesisi446 – 4472RR → AA: Reduces nick joining activity by 95%. 1 Publication
Mutagenesisi455 – 4551G → A: Reduces nick joining activity by 50%. 1 Publication
Mutagenesisi455 – 4551G → D or V: Reduces nick joining activity by 95%. 1 Publication
Mutagenesisi487 – 4871R → A: Reduces nick joining activity by over 90%. 1 Publication
Mutagenesisi489 – 4891G → D or V: Reduces nick joining activity by 95%. 1 Publication
Mutagenesisi521 – 5211G → A: Reduces nick joining activity by 95%. 1 Publication
Mutagenesisi521 – 5211G → D or V: Loss of nick joining activity. 1 Publication
Mutagenesisi553 – 5531G → D or V: Reduces nick joining activity by 95%. 1 Publication
Mutagenesisi614 – 6141R → A: Reduces nick joining activity by 85%. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 671671DNA ligasePRO_0000161745Add
BLAST

Proteomic databases

PaxDbiP15042.
PRIDEiP15042.

Expressioni

Gene expression databases

GenevestigatoriP15042.

Interactioni

Protein-protein interaction databases

DIPiDIP-10098N.
IntActiP15042. 20 interactions.
MINTiMINT-204717.
STRINGi511145.b2411.

Structurei

Secondary structure

1
671
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 2421
Beta strandi28 – 303
Helixi34 – 4815
Helixi50 – 523
Helixi58 – 603
Beta strandi72 – 743
Beta strandi83 – 853
Helixi88 – 10013
Beta strandi102 – 1043
Beta strandi110 – 12617
Beta strandi129 – 1357
Beta strandi139 – 1446
Helixi146 – 1494
Beta strandi161 – 1633
Beta strandi166 – 17510
Helixi178 – 19013
Helixi199 – 2079
Helixi212 – 2165
Beta strandi221 – 23313
Helixi239 – 24810
Beta strandi258 – 2625
Helixi263 – 27614
Helixi277 – 2793
Beta strandi280 – 2823
Beta strandi284 – 29310
Helixi294 – 3007
Beta strandi304 – 31310
Beta strandi319 – 33113
Beta strandi335 – 34814
Beta strandi351 – 3577
Helixi361 – 3677
Beta strandi374 – 3807
Turni381 – 3833
Beta strandi384 – 3907
Helixi392 – 3943
Turni409 – 4113
Beta strandi414 – 4163
Beta strandi425 – 4273
Helixi429 – 4313
Helixi433 – 44412
Turni446 – 4494
Helixi456 – 4649
Helixi471 – 4755
Helixi479 – 4835
Helixi490 – 50314
Helixi508 – 5147
Helixi522 – 53211
Helixi535 – 5406
Helixi543 – 5464
Helixi554 – 56512
Helixi567 – 57812

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OWOX-ray2.30A1-671[»]
4GLXX-ray1.90A1-586[»]
ProteinModelPortaliP15042.
SMRiP15042. Positions 1-586, 600-669.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15042.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini593 – 67179BRCTAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni330 – 3345Interaction with target DNA
Regioni453 – 4586Interaction with target DNA
Regioni519 – 5246Interaction with target DNA
Regioni551 – 5566Interaction with target DNA

Sequence similaritiesi

Contains 1 BRCT domain.Curated

Phylogenomic databases

eggNOGiCOG0272.
HOGENOMiHOG000218459.
InParanoidiP15042.
KOiK01972.
OMAiFPAQEQL.
OrthoDBiEOG6TTVM9.
PhylomeDBiP15042.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
3.40.50.10190. 1 hit.
HAMAPiMF_01588. DNA_ligase_A.
InterProiIPR001357. BRCT_dom.
IPR018239. DNA_ligase_AS.
IPR001679. DNAligase.
IPR013839. DNAligase_adenylation.
IPR013840. DNAligase_N.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR012340. NA-bd_OB-fold.
IPR004150. NAD_DNA_ligase_OB.
IPR010994. RuvA_2-like.
IPR004149. Znf_DNAligase_C4.
[Graphical view]
PfamiPF00533. BRCT. 1 hit.
PF01653. DNA_ligase_aden. 1 hit.
PF03120. DNA_ligase_OB. 1 hit.
PF03119. DNA_ligase_ZBD. 1 hit.
[Graphical view]
PIRSFiPIRSF001604. LigA. 1 hit.
SMARTiSM00292. BRCT. 1 hit.
SM00278. HhH1. 4 hits.
SM00532. LIGANc. 1 hit.
[Graphical view]
SUPFAMiSSF47781. SSF47781. 1 hit.
SSF50249. SSF50249. 1 hit.
SSF52113. SSF52113. 1 hit.
TIGRFAMsiTIGR00575. dnlj. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
PS01055. DNA_LIGASE_N1. 1 hit.
PS01056. DNA_LIGASE_N2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P15042 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MESIEQQLTE LRTTLRHHEY LYHVMDAPEI PDAEYDRLMR ELRELETKHP
60 70 80 90 100
ELITPDSPTQ RVGAAPLAAF SQIRHEVPML SLDNVFDEES FLAFNKRVQD
110 120 130 140 150
RLKNNEKVTW CCELKLDGLA VSILYENGVL VSAATRGDGT TGEDITSNVR
160 170 180 190 200
TIRAIPLKLH GENIPARLEV RGEVFLPQAG FEKINEDARR TGGKVFANPR
210 220 230 240 250
NAAAGSLRQL DPRITAKRPL TFFCYGVGVL EGGELPDTHL GRLLQFKKWG
260 270 280 290 300
LPVSDRVTLC ESAEEVLAFY HKVEEDRPTL GFDIDGVVIK VNSLAQQEQL
310 320 330 340 350
GFVARAPRWA VAFKFPAQEQ MTFVRDVEFQ VGRTGAITPV ARLEPVHVAG
360 370 380 390 400
VLVSNATLHN ADEIERLGLR IGDKVVIRRA GDVIPQVVNV VLSERPEDTR
410 420 430 440 450
EVVFPTHCPV CGSDVERVEG EAVARCTGGL ICGAQRKESL KHFVSRRAMD
460 470 480 490 500
VDGMGDKIID QLVEKEYVHT PADLFKLTAG KLTGLERMGP KSAQNVVNAL
510 520 530 540 550
EKAKETTFAR FLYALGIREV GEATAAGLAA YFGTLEALEA ASIEELQKVP
560 570 580 590 600
DVGIVVASHV HNFFAEESNR NVISELLAEG VHWPAPIVIN AEEIDSPFAG
610 620 630 640 650
KTVVLTGSLS QMSRDDAKAR LVELGAKVAG SVSKKTDLVI AGEAAGSKLA
660 670
KAQELGIEVI DEAEMLRLLG S
Length:671
Mass (Da):73,606
Last modified:November 1, 1997 - v2
Checksum:iDD2BDC64D8E65256
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691A → R in AAA24071. (PubMed:3018436)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M30255 Genomic DNA. Translation: AAA24071.1.
M24278 Genomic DNA. Translation: AAA24070.1.
U00096 Genomic DNA. Translation: AAC75464.1.
AP009048 Genomic DNA. Translation: BAA16282.2.
U74650 Genomic DNA. Translation: AAB42062.1.
PIRiB65015. LQECC6.
RefSeqiNP_416906.1. NC_000913.3.
YP_490647.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75464; AAC75464; b2411.
BAA16282; BAA16282; BAA16282.
GeneIDi12930678.
946885.
KEGGiecj:Y75_p2372.
eco:b2411.
PATRICi32120205. VBIEscCol129921_2505.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M30255 Genomic DNA. Translation: AAA24071.1 .
M24278 Genomic DNA. Translation: AAA24070.1 .
U00096 Genomic DNA. Translation: AAC75464.1 .
AP009048 Genomic DNA. Translation: BAA16282.2 .
U74650 Genomic DNA. Translation: AAB42062.1 .
PIRi B65015. LQECC6.
RefSeqi NP_416906.1. NC_000913.3.
YP_490647.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2OWO X-ray 2.30 A 1-671 [» ]
4GLX X-ray 1.90 A 1-586 [» ]
ProteinModelPortali P15042.
SMRi P15042. Positions 1-586, 600-669.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10098N.
IntActi P15042. 20 interactions.
MINTi MINT-204717.
STRINGi 511145.b2411.

Proteomic databases

PaxDbi P15042.
PRIDEi P15042.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75464 ; AAC75464 ; b2411 .
BAA16282 ; BAA16282 ; BAA16282 .
GeneIDi 12930678.
946885.
KEGGi ecj:Y75_p2372.
eco:b2411.
PATRICi 32120205. VBIEscCol129921_2505.

Organism-specific databases

EchoBASEi EB0529.
EcoGenei EG10534. ligA.

Phylogenomic databases

eggNOGi COG0272.
HOGENOMi HOG000218459.
InParanoidi P15042.
KOi K01972.
OMAi FPAQEQL.
OrthoDBi EOG6TTVM9.
PhylomeDBi P15042.

Enzyme and pathway databases

BioCyci EcoCyc:EG10534-MONOMER.
ECOL316407:JW2403-MONOMER.
MetaCyc:EG10534-MONOMER.

Miscellaneous databases

EvolutionaryTracei P15042.
PROi P15042.

Gene expression databases

Genevestigatori P15042.

Family and domain databases

Gene3Di 2.40.50.140. 1 hit.
3.40.50.10190. 1 hit.
HAMAPi MF_01588. DNA_ligase_A.
InterProi IPR001357. BRCT_dom.
IPR018239. DNA_ligase_AS.
IPR001679. DNAligase.
IPR013839. DNAligase_adenylation.
IPR013840. DNAligase_N.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR012340. NA-bd_OB-fold.
IPR004150. NAD_DNA_ligase_OB.
IPR010994. RuvA_2-like.
IPR004149. Znf_DNAligase_C4.
[Graphical view ]
Pfami PF00533. BRCT. 1 hit.
PF01653. DNA_ligase_aden. 1 hit.
PF03120. DNA_ligase_OB. 1 hit.
PF03119. DNA_ligase_ZBD. 1 hit.
[Graphical view ]
PIRSFi PIRSF001604. LigA. 1 hit.
SMARTi SM00292. BRCT. 1 hit.
SM00278. HhH1. 4 hits.
SM00532. LIGANc. 1 hit.
[Graphical view ]
SUPFAMi SSF47781. SSF47781. 1 hit.
SSF50249. SSF50249. 1 hit.
SSF52113. SSF52113. 1 hit.
TIGRFAMsi TIGR00575. dnlj. 1 hit.
PROSITEi PS50172. BRCT. 1 hit.
PS01055. DNA_LIGASE_N1. 1 hit.
PS01056. DNA_LIGASE_N2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the lig gene and primary structure of DNA ligase of Escherichia coli."
    Ishino Y., Shinagawa H., Makino K., Tsunasawa S., Sakiyama F., Nakata A.
    Mol. Gen. Genet. 204:1-7(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-13 AND 666-671.
    Strain: K12 / C600 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222.
  2. O'Connor M.J., Ally A., Ally D., Zhang X., Robichaud M., Backman K.
    Submitted (APR-1989) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. coli."
    Hale C.A., de Boer P.A.J.
    Cell 88:175-185(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-90.
    Strain: PB103.
  7. "Conserved residues in domain Ia are required for the reaction of Escherichia coli DNA ligase with NAD+."
    Sriskanda V., Shuman S.
    J. Biol. Chem. 277:9695-9700(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF GLU-10; TYR-22; HIS-23; ASP-32; TYR-35 AND ASP-36, ACTIVE SITE.
  8. "Structure-guided mutational analysis of the nucleotidyltransferase domain of Escherichia coli NAD+-dependent DNA ligase (LigA)."
    Zhu H., Shuman S.
    J. Biol. Chem. 280:12137-12144(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LYS-115; ASP-117; GLY-118; ASP-138; GLU-143; GLY-172; GLU-173; ASN-198; ARG-200; ARG-208; ARG-277; ASP-285; GLY-286; VAL-288; LYS-290 AND LYS-314.
  9. "Structure-guided mutational analysis of the OB, HhH, and BRCT domains of Escherichia coli DNA ligase."
    Wang L.K., Nair P.A., Shuman S.
    J. Biol. Chem. 283:23343-23352(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ARG-333; THR-334; ARG-342; ARG-379; 383-VAL-ILE-384; 446-ARG-ARG-447; GLY-455; ARG-487; GLY-489; GLY-521; GLY-553 AND ARG-614.
  10. "Last stop on the road to repair: structure of E. coli DNA ligase bound to nicked DNA-adenylate."
    Nandakumar J., Nair P.A., Shuman S.
    Mol. Cell 26:257-271(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH ZINC IONS; AMP AND DNA.

Entry informationi

Entry nameiDNLJ_ECOLI
AccessioniPrimary (citable) accession number: P15042
Secondary accession number(s): P78197, P78198
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1997
Last modified: October 29, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3