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2OWO

Last Stop on the Road to Repair: Structure of E.coli DNA Ligase Bound to Nicked DNA-Adenylate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003911molecular_functionDNA ligase (NAD+) activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006259biological_processDNA metabolic process
A0006260biological_processDNA replication
A0006266biological_processDNA ligation
A0006281biological_processDNA repair
A0006288biological_processbase-excision repair, DNA ligation
A0016874molecular_functionligase activity
A0046872molecular_functionmetal ion binding
A0070403molecular_functionNAD+ binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 672
ChainResidue
ACYS408
ACYS411
ACYS426
ACYS432

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 673
ChainResidue
AARG446
AARG447
AHOH922
CHOH42
DDC40

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 674
ChainResidue
AARG74
AARG510
AHOH718
AHOH759

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 675
ChainResidue
AASN95
AGLN99
ASER262
AALA263
AHOH799

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 676
ChainResidue
AHIS559
AASN562

site_idAC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE AMP D 53
ChainResidue
ASER81
ALEU82
AGLU113
ALYS115
AALA120
AARG136
AGLU173
ATYR225
AVAL288
ALYS290
AHOH752
CHOH137
DDC40

Functional Information from PROSITE/UniProt
site_idPS01055
Number of Residues30
DetailsDNA_LIGASE_N1 NAD-dependent DNA ligase signature 1. KLDGLAvsilYenGvLvsaaTRGDGttGED
ChainResidueDetails
ALYS115-ASP144

site_idPS01056
Number of Residues16
DetailsDNA_LIGASE_N2 NAD-dependent DNA ligase signature 2. VGRTGaITpVarLePV
ChainResidueDetails
AVAL331-VAL346

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: N6-AMP-lysine intermediate => ECO:0000255|HAMAP-Rule:MF_01588, ECO:0000269|PubMed:11781321
ChainResidueDetails
ALYS115

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01588
ChainResidueDetails
AASP32
AGLU173
ALYS314

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01588, ECO:0000305|PubMed:17466627
ChainResidueDetails
ASER81
AGLU113
AARG136
ALYS290

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01588, ECO:0000269|PubMed:17466627
ChainResidueDetails
ACYS408
ACYS411
ACYS426
ACYS432

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Interaction with target DNA => ECO:0000305|PubMed:17466627
ChainResidueDetails
AARG487
ASER492

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1b04
ChainResidueDetails
ALYS115

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1b04
ChainResidueDetails
AARG200
AASP117
ALYS314
ALYS115

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PDB entries from 2024-07-24

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