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2P4Q

Crystal Structure Analysis of Gnd1 in Saccharomyces cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0004616molecular_functionphosphogluconate dehydrogenase (decarboxylating) activity
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006098biological_processpentose-phosphate shunt
A0009051biological_processpentose-phosphate shunt, oxidative branch
A0016491molecular_functionoxidoreductase activity
A0019521biological_processD-gluconate metabolic process
A0034599biological_processcellular response to oxidative stress
A0046177biological_processD-gluconate catabolic process
A0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE FLC A 501
ChainResidue
AGLU189
AFLC502
ATYR190
AMET193
AGLN258
ALYS259
ATHR261
AARG286
AARG446
AHIS452

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE FLC A 502
ChainResidue
AASN102
ASER128
AGLY130
ALYS182
AHIS185
AASN186
AGLU189
AILE366
AHIS452
AFLC501

Functional Information from PROSITE/UniProt
site_idPS00461
Number of Residues13
Details6PGD 6-phosphogluconate dehydrogenase signature. ImDtaGQKGTGkW
ChainResidueDetails
AILE252-TRP264

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
ALYS182

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLU189

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASN32
AVAL74
AARG446
AHIS452
AGLY9

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: in other chain => ECO:0000250
ChainResidueDetails
AASN102
ATYR190
ALYS259
AARG286
ASER128
AHIS185

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER50

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PDB entries from 2024-06-12

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