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2IYO

Structural characterization of a bacterial 6PDH reveals aspects of specificity, mechanism and mode of inhibition

Functional Information from GO Data
ChainGOidnamespacecontents
A0004616molecular_functionphosphogluconate dehydrogenase (decarboxylating) activity
A0005829cellular_componentcytosol
A0006098biological_processpentose-phosphate shunt
A0008114molecular_functionphosphogluconate 2-dehydrogenase activity
A0009051biological_processpentose-phosphate shunt, oxidative branch
A0016054biological_processorganic acid catabolic process
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 Residues19
DetailsBINDING SITE FOR RESIDUE 6PG A1471
ChainResidue
AASN102
ALYS262
AARG289
AILE367
AARG447
APHE450
AHIS453
AHOH2115
AHOH2311
AHOH2312
AHOH2313
ASER128
AGLY129
AGLY130
ALYS184
AHIS187
AASN188
AGLU191
ATYR192

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CAC A1472
ChainResidue
ALYS262
AGLY451
AALA452
AHIS453

Functional Information from PROSITE/UniProt
site_idPS00461
Number of Residues13
Details6PGD 6-phosphogluconate dehydrogenase signature. IlDkaGNKGTGkW
ChainResidueDetails
AILE255-TRP267

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:17222187
ChainResidueDetails
ALYS184

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:17222187
ChainResidueDetails
AGLU191

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:17222187
ChainResidueDetails
AGLY10
AASN33
AVAL74
AARG447
AHIS453

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: in other chain => ECO:0000269|PubMed:17222187
ChainResidueDetails
AASN102
ASER128
AHIS187
ATYR192
ALYS262
AARG289

218853

PDB entries from 2024-04-24

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