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4ESE

The crystal structure of azoreductase from Yersinia pestis CO92 in complex with FMN.

Functional Information from GO Data
ChainGOidnamespacecontents
A0009055molecular_functionelectron transfer activity
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
A0016652molecular_functionoxidoreductase activity, acting on NAD(P)H as acceptor
A0016655molecular_functionoxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE FMN A 301
ChainResidue
AASN98
AHOH538
AHOH543
AHOH567
AHOH585
APHE163
APRO181
AGLU182
AVAL183
ALYS186
AFMN302
AHOH401
AHOH533

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE FMN A 302
ChainResidue
ASER10
ALEU12
ASER16
AGLN17
ASER18
APRO95
AMET96
ATYR97
AASN98
APHE99
ASER140
AFMN301
AHOH493
AHOH540

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FMN A 303
ChainResidue
AARG134
AARG141
AVAL154
AARG158
AASP168
AGLU170
APHE171
APHE173
AGLN197

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE 12P A 304
ChainResidue
AALA44
AARG69
AHOH416
AHOH549

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 305
ChainResidue
AGLU182
AVAL183
AALA184
ATHR185
ALYS186
AALA187
AGLN188

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE IMD A 306
ChainResidue
AASN100
AASN100
ALEU152
ALEU152
AHOH589
AHOH589

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000269|Ref.4, ECO:0007744|PDB:4ESE
ChainResidueDetails
ASER10
ASER16
AMET96

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01216
ChainResidueDetails
ASER140

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PDB entries from 2024-10-09

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