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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
A0005829cellular_componentcytosol
A0006098biological_processpentose-phosphate shunt
A0008114molecular_functionphosphogluconate 2-dehydrogenase activity
A0009051biological_processpentose-phosphate shunt, oxidative branch
A0016491molecular_functionoxidoreductase activity
A0019521biological_processD-gluconate metabolic process
A0046177biological_processD-gluconate catabolic process
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
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AMET184

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
ATYR191

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: in other chain
ChainResidueDetails
ALEU10
ACYS288
AARG33
ALYS75
ASER103
AGLY129
AGLU131
AASN187
AGLY192
AGLY261

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP447
ATHR453
ASER478

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9DCD0
ChainResidueDetails
AVAL38

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9DCD0
ChainResidueDetails
ALEU57
AGLY129

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 889
ChainResidueDetails
AGLY129electrostatic stabiliser, promote heterolysis
AMET184proton acceptor, proton donor
AASN187electrostatic stabiliser, promote heterolysis
AGLY188electrostatic stabiliser, promote heterolysis
ATYR191proton acceptor, proton donor

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PDB entries from 2024-04-24

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