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4EEQ

Crystal structure of E. faecalis DNA ligase with inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0003911molecular_functionDNA ligase (NAD+) activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 401
ChainResidue
AGLY123
AHOH865
ALEU124
AALA125
AARG141
AARG202
AHOH554
AHOH579
AHOH770
AHOH811

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 402
ChainResidue
AARG129
AARG137
AHOH511
AHOH665
AHOH871

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE NMN A 403
ChainResidue
ATYR25
ATYR29
ATYR30
AVAL37
AASP39
ATYR42
AASP43
ATYR46
AARG158
AHOH502
AHOH537
AHOH627
AHOH637
AHOH646
AHOH706
AHOH823
AHOH828

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 0OX A 404
ChainResidue
ALEU89
AGLU118
ALEU119
ALYS120
AILE121
ATYR227
ALYS291
ATRP310
AHOH590
AHOH605
AHOH751
AHOH889
AHOH898

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
AASP39
ASER88
AGLU118
AARG141
AGLU175
ALYS291
ALYS315

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PDB entries from 2024-07-24

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