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1HW6

CRYSTAL STRUCTURE OF APO-2,5-DIKETO-D-GLUCONATE REDUCTASE

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 Residues6
DetailsBINDING SITE FOR RESIDUE MG A 300
ChainResidue
AASP252
AHOH456
AHOH470
AHOH475
AHOH504
AHOH507

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 301
ChainResidue
AHOH619
AHOH623
AHIS180
AHOH561
AHOH577

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 422
ChainResidue
AARG67
AASP100
AGLN101

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 424
ChainResidue
AGLY188
ALEU190
AGLN192

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

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PDB entries from 2024-10-09

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