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1M9H

Corynebacterium 2,5-DKGR A and Phe 22 replaced with Tyr (F22Y), Lys 232 replaced with Gly (K232G), Arg 238 replaced with His (R238H)and Ala 272 replaced with Gly (A272G)in presence of NADH cofactor

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 Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
AILE6
AVAL7
ALYS183
AARG220
APHE246
AHOH325
AHOH337
AHOH338

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE NAD A 300
ChainResidue
AVAL21
ATYR22
AASP45
ATYR50
AHIS108
ASER139
AASN140
AGLN161
ATRP187
AGLY188
APRO189
ALEU190
AGLY191
AGLN192
APHE198
AALA215
APHE230
APRO231
AGLY232
ASER233
AHIS238
AGLU241
AASN242
AHOH382
AGLY20

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
AGLY51

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:11399090
ChainResidueDetails
ATRP109

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:14718658
ChainResidueDetails
APRO189

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

225946

PDB entries from 2024-10-09

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