1PGJ
X-RAY STRUCTURE OF 6-PHOSPHOGLUCONATE DEHYDROGENASE FROM THE PROTOZOAN PARASITE T. BRUCEI
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004616 | molecular_function | phosphogluconate dehydrogenase (decarboxylating) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006098 | biological_process | pentose-phosphate shunt |
| A | 0008114 | molecular_function | phosphogluconate 2-dehydrogenase activity |
| A | 0009051 | biological_process | pentose-phosphate shunt, oxidative branch |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019521 | biological_process | D-gluconate metabolic process |
| A | 0020015 | cellular_component | glycosome |
| A | 0046177 | biological_process | D-gluconate catabolic process |
| A | 0050661 | molecular_function | NADP binding |
| A | 0097014 | cellular_component | ciliary plasm |
| B | 0004616 | molecular_function | phosphogluconate dehydrogenase (decarboxylating) activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006098 | biological_process | pentose-phosphate shunt |
| B | 0008114 | molecular_function | phosphogluconate 2-dehydrogenase activity |
| B | 0009051 | biological_process | pentose-phosphate shunt, oxidative branch |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019521 | biological_process | D-gluconate metabolic process |
| B | 0020015 | cellular_component | glycosome |
| B | 0046177 | biological_process | D-gluconate catabolic process |
| B | 0050661 | molecular_function | NADP binding |
| B | 0097014 | cellular_component | ciliary plasm |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 505 |
| Chain | Residue |
| A | TYR193 |
| A | SER261 |
| A | LYS262 |
| A | ARG289 |
| A | HOH542 |
| B | ARG453 |
| B | HIS459 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 507 |
| Chain | Residue |
| A | ASN189 |
| A | HOH519 |
| A | HOH555 |
| A | ASN104 |
| A | LYS185 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 505 |
| Chain | Residue |
| A | ARG453 |
| A | HIS459 |
| B | TYR193 |
| B | SER261 |
| B | LYS262 |
| B | ARG289 |
| B | HOH554 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 507 |
| Chain | Residue |
| B | ASN104 |
| B | LYS185 |
| B | ASN189 |
| B | HOH521 |
Functional Information from PROSITE/UniProt
| site_id | PS00461 |
| Number of Residues | 13 |
| Details | 6PGD 6-phosphogluconate dehydrogenase signature. VmDriGSKGTGlW |
| Chain | Residue | Details |
| A | VAL255-TRP267 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS185 | |
| B | LYS185 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU192 | |
| B | GLU192 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLY8 | |
| B | HIS459 | |
| A | ASN31 | |
| A | VAL76 | |
| A | ARG453 | |
| A | HIS459 | |
| B | GLY8 | |
| B | ASN31 | |
| B | VAL76 | |
| B | ARG453 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | BINDING: in other chain => ECO:0000250 |
| Chain | Residue | Details |
| A | ASN104 | |
| B | TYR193 | |
| B | LYS262 | |
| B | ARG289 | |
| A | SER130 | |
| A | HIS188 | |
| A | TYR193 | |
| A | LYS262 | |
| A | ARG289 | |
| B | ASN104 | |
| B | SER130 | |
| B | HIS188 |
