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1PGP

CRYSTALLOGRAPHIC STUDY OF COENZYME, COENZYME ANALOGUE AND SUBSTRATE BINDING IN 6-PHOSPHOGLUCONATE DEHYDROGENASE: IMPLICATIONS FOR NADP SPECIFICITY AND THE ENZYME MECHANISM

Functional Information from GO Data
ChainGOidnamespacecontents
A0004616molecular_functionphosphogluconate dehydrogenase (decarboxylating) activity
A0005737cellular_componentcytoplasm
A0006098biological_processpentose-phosphate shunt
A0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 6PG A 502
ChainResidue
AASN102
AARG287
AILE366
AARG446
AHIS452
AHOH528
AHOH1109
AHOH1232
ASER128
AGLY129
ALYS183
AASN187
AGLU190
ATYR191
ALYS260
ATHR262

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 508
ChainResidue
ALYS50
AGLY211
AHIS212
AHIS248
AHOH636
AHOH1164

Functional Information from PROSITE/UniProt
site_idPS00461
Number of Residues13
Details6PGD 6-phosphogluconate dehydrogenase signature. IrDsaGQKGTGkW
ChainResidueDetails
AILE253-TRP265

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"7922042","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7922042","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PGO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues5
DetailsBinding site: {"description":"in chain A","evidences":[{"source":"PubMed","id":"7922042","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PGP","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"description":"in chain B","evidences":[{"source":"PubMed","id":"7922042","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PGP","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P52209","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9DCD0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9DCD0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 2pgd
ChainResidueDetails
AASN187
ALYS183
AGLY130
AGLU190

site_idMCSA1
Number of Residues5
DetailsM-CSA 889
ChainResidueDetails
ASER128electrostatic stabiliser, promote heterolysis
ALYS183proton acceptor, proton donor
AHIS186electrostatic stabiliser, promote heterolysis
AASN187electrostatic stabiliser, promote heterolysis
AGLU190proton acceptor, proton donor

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PDB entries from 2026-09-30

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