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4GWK

Crystal structure of 6-phosphogluconate dehydrogenase complexed with 3-phosphoglyceric acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0004616molecular_functionphosphogluconate dehydrogenase (decarboxylating) activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006098biological_processpentose-phosphate shunt
A0009051biological_processpentose-phosphate shunt, oxidative branch
A0016491molecular_functionoxidoreductase activity
A0019322biological_processpentose biosynthetic process
A0019521biological_processD-gluconate metabolic process
A0046177biological_processD-gluconate catabolic process
A0050661molecular_functionNADP binding
A0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 3PG A 501
ChainResidue
AALA212
AGLN213
ALYS248
AHIS249
APRO252
AHOH682
AHOH757
AHOH895

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MES A 502
ChainResidue
AARG107
AMET185
ATRP266
AHOH625
AHOH639
AHOH689
AGLU105

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MES A 503
ChainResidue
AGLY131
AGLU132
AGLY167
AGLU168
AGLY451
AALA452

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 3PG A 504
ChainResidue
AGLU191
ATYR192
ALYS261
AGLY262
ATHR263
AARG288
AARG447
AHOH628
AHOH651
AHOH793
AHOH817

Functional Information from PROSITE/UniProt
site_idPS00461
Number of Residues13
Details6PGD 6-phosphogluconate dehydrogenase signature. IrDsaGQKGTGkW
ChainResidueDetails
AILE254-TRP266

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
ALYS184

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLU191

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: in other chain => ECO:0000269|Ref.9
ChainResidueDetails
AGLY10
AASN33
AVAL75

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: in other chain => ECO:0000250
ChainResidueDetails
AASN103
ASER129
AHIS187
ATYR192
ALYS261
AARG288

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AARG447
AHIS453

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|Ref.9
ChainResidueDetails
ASER478

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9DCD0
ChainResidueDetails
ALYS38

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9DCD0
ChainResidueDetails
ASER57
ASER129

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS59
ALYS309

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PDB entries from 2024-07-10

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