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3RQ6

Crystal Structure of ADP/ATP-dependent NAD(P)H-hydrate dehydratase from Bacillus subtilis soaked with ADP-ribose

Functional Information from GO Data
ChainGOidnamespacecontents
A0016836molecular_functionhydro-lyase activity
A0046496biological_processnicotinamide nucleotide metabolic process
A0052855molecular_functionADP-dependent NAD(P)H-hydrate dehydratase activity
A0052856molecular_functionNAD(P)HX epimerase activity
A0110051biological_processmetabolite repair
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 277
ChainResidue
ALYS186
AAPR278
AHOH298
AHOH309
AHOH360
AHOH371

site_idAC2
Number of Residues31
DetailsBINDING SITE FOR RESIDUE APR A 278
ChainResidue
AGLU76
AHIS149
ALYS186
AGLY187
AASN188
ATHR190
AASN206
AGLY207
ALEU209
AALA210
AGLY212
AGLY213
ATHR214
AGLY215
AASP216
AHIS243
AMG277
AHOH288
AHOH298
AHOH309
AHOH311
AHOH321
AHOH338
AHOH360
AHOH371
AHOH396
AHOH413
AHOH440
AALA20
ASER22
ALYS24

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE APR A 279
ChainResidue
ATYR79
ATRP80
ALYS86
ALEU92
AGLU93
AGLU94
ATYR96
AHOH306
AHOH420
AHOH425

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 Residues268
DetailsDomain: {"description":"YjeF C-terminal","evidences":[{"source":"HAMAP-Rule","id":"MF_01965","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22940582","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3RPZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

251422

PDB entries from 2026-04-01

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