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3RQ5

Crystal Structure of ADP/ATP-dependent NAD(P)H-hydrate dehydratase from Bacillus subtilis co-crystallized with ATP/Mg2+ and soaked with CoA

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
A0046496biological_processnicotinamide nucleotide metabolic process
A0052855molecular_functionADP-dependent NAD(P)H-hydrate dehydratase activity
A0052856molecular_functionNADHX epimerase activity
A0052857molecular_functionNADPHX epimerase activity
A0110051biological_processmetabolite repair
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE COA A 277
ChainResidue
ATYR27
AGLY215
AASP216
AHOH308
AHOH324
AHOH352
AHOH364
AHOH366
AHOH427
AHOH428
AHOH429
ATHR29
AGLY56
ALYS57
AHIS149
AALA210
AGLY212
AGLY213
ATHR214

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 278
ChainResidue
AASP37
APRO40
APRO68
AARG81
AHOH325
AHOH390

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 279
ChainResidue
ATRP80
ALEU92
AGLU93
AGLU94
ATYR96

Functional Information from PROSITE/UniProt
site_idPS01049
Number of Residues11
DetailsYJEF_C_1 YjeF C-terminal domain signature 1. AIAIGPGLPqT
ChainResidueDetails
AALA98-THR108

site_idPS01050
Number of Residues11
DetailsYJEF_C_2 YjeF C-terminal domain signature 2. GGtGDTLTGmI
ChainResidueDetails
AGLY212-ILE222

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:22940582, ECO:0007744|PDB:3RPZ
ChainResidueDetails
AALA42
AGLY104
AHIS149
ALYS186
AGLY215
AASP216

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PDB entries from 2024-07-24

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