2ZYD
Dimeric 6-phosphogluconate dehydrogenase complexed with glucose
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004616 | molecular_function | phosphogluconate dehydrogenase (decarboxylating) activity |
A | 0005829 | cellular_component | cytosol |
A | 0006098 | biological_process | pentose-phosphate shunt |
A | 0009051 | biological_process | pentose-phosphate shunt, oxidative branch |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0019521 | biological_process | D-gluconate metabolic process |
A | 0042802 | molecular_function | identical protein binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0050661 | molecular_function | NADP binding |
A | 0097216 | molecular_function | guanosine tetraphosphate binding |
B | 0004616 | molecular_function | phosphogluconate dehydrogenase (decarboxylating) activity |
B | 0005829 | cellular_component | cytosol |
B | 0006098 | biological_process | pentose-phosphate shunt |
B | 0009051 | biological_process | pentose-phosphate shunt, oxidative branch |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
B | 0019521 | biological_process | D-gluconate metabolic process |
B | 0042802 | molecular_function | identical protein binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0050661 | molecular_function | NADP binding |
B | 0097216 | molecular_function | guanosine tetraphosphate binding |
Functional Information from PROSITE/UniProt
site_id | PS00461 |
Number of Residues | 13 |
Details | 6PGD 6-phosphogluconate dehydrogenase signature. IlDeaANKGTGkW |
Chain | Residue | Details |
A | ILE253-TRP265 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"19686854","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"19686854","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 22 |
Details | Binding site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 10 |
Details | Binding site: {"description":"in other chain"} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | Binding site: {"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 2pgd |
Chain | Residue | Details |
A | ASN187 | |
A | LYS183 | |
A | GLY130 | |
A | GLU190 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 2pgd |
Chain | Residue | Details |
B | ASN187 | |
B | LYS183 | |
B | GLY130 | |
B | GLU190 |