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1A80

Native 2,5-DIKETO-D-GLUCONIC acid reductase a from CORYNBACTERIUM SP. complexed with nadph

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0019853biological_processL-ascorbic acid biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues31
DetailsBINDING SITE FOR RESIDUE NDP A 300
ChainResidue
AGLY20
AVAL21
APHE22
AASP45
ATYR50
ALYS75
AHIS108
ASER139
AASN140
AGLN161
ATRP187
AGLY188
APRO189
ALEU190
AGLY191
AGLN192
AALA215
APHE230
APRO231
ALYS232
ASER233
AVAL234
AARG235
AARG238
AGLU241
AASN242
AHOH332
AHOH342
AHOH352
AHOH396
AHOH406

site_idCIC
Number of Residues9
DetailsTHE RESIDUE LINE THE ACTIVE SITE OF THE ENZYME.
ChainResidue
APHE22
AASP45
AALA47
ATYR50
ALYS75
ALEU106
ASER139
AASN140
ATRP187

Functional Information from PROSITE/UniProt
site_idPS00798
Number of Residues18
DetailsALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRHIDTAaiygnEegVG
ChainResidueDetails
AGLY40-GLY57

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:11399090
ChainResidueDetails
ATYR50

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:11399090
ChainResidueDetails
AHIS108

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:14718658
ChainResidueDetails
AGLY188

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mrq
ChainResidueDetails
ALYS75
AASP45
ATYR50
AHIS108

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mrq
ChainResidueDetails
ALYS75
ATYR50

226707

PDB entries from 2024-10-30

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