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2PGD

THE STRUCTURE OF 6-PHOSPHOGLUCONATE DEHYDROGENASE REFINED AT 2 ANGSTROMS RESOLUTION

Replaces:  1PGD
Functional Information from GO Data
ChainGOidnamespacecontents
A0004616molecular_functionphosphogluconate dehydrogenase (decarboxylating) activity
A0005737cellular_componentcytoplasm
A0006098biological_processpentose-phosphate shunt
A0016491molecular_functionoxidoreductase activity
A0019521biological_processD-gluconate metabolic process
A0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 505
ChainResidue
ATYR191
ALYS260
AARG287
AARG446
AHIS452
AHOH528
AHOH886
AHOH953

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 507
ChainResidue
ALYS183
AASN187
AHOH613
AHOH614
AHOH699
AASN102

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 508
ChainResidue
ALYS50
AGLY211
AHIS212
AHIS248
AHOH636
AHOH899

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"}
ChainResidueDetails

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

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"description":"in other chain"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9DCD0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
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
Details
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 2025-07-16

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