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3BA8

Structural Basis for the Inhibition of Bacterial NAD+ Dependent DNA Ligase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003911molecular_functionDNA ligase (NAD+) activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 402
ChainResidue
ALEU124
AALA125
AARG141
AHOH527
AHOH560
AHOH567
AHOH641

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 403
ChainResidue
AARG137
AHOH522
AHOH695
AHOH733
APRO81
AARG129

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 404
ChainResidue
AARG190
AGLN195
AGLN211
AARG220
AHOH556

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE NMN A 401
ChainResidue
ATYR25
ATYR29
ATYR30
AVAL37
AASP39
ATYR42
AASP43
AARG158
AHOH507
AHOH593
AHOH612

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 3B8 A 501
ChainResidue
ATYR87
ALEU89
AGLU118
ALEU119
ALYS120
AILE121
AARG141
AGLU175
ATYR227
ALYS291
APRO308
ATRP310

Functional Information from PROSITE/UniProt
site_idPS01055
Number of Residues30
DetailsDNA_LIGASE_N1 NAD-dependent DNA ligase signature 1. KIDGLAislrYenGvFvrgaTRGDGtvGEN
ChainResidueDetails
ALYS120-ASN149

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: N6-AMP-lysine intermediate => ECO:0000255|HAMAP-Rule:MF_01588
ChainResidueDetails
ALYS120

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01588, ECO:0000269|PubMed:15296738
ChainResidueDetails
ASER88
AGLU118
AARG141
AGLU175
ALYS291
ALYS315
AASP39

219869

PDB entries from 2024-05-15

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