1TZC
Crystal structure of phosphoglucose/phosphomannose isomerase from Pyrobaculum aerophilum in complex with 5-phosphoarabinonate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004347 | molecular_function | glucose-6-phosphate isomerase activity |
| A | 0004476 | molecular_function | mannose-6-phosphate isomerase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0097367 | molecular_function | carbohydrate derivative binding |
| A | 1901135 | biological_process | carbohydrate derivative metabolic process |
| B | 0004347 | molecular_function | glucose-6-phosphate isomerase activity |
| B | 0004476 | molecular_function | mannose-6-phosphate isomerase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0097367 | molecular_function | carbohydrate derivative binding |
| B | 1901135 | biological_process | carbohydrate derivative metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 451 |
| Chain | Residue |
| A | ARG181 |
| A | ARG284 |
| A | HOH780 |
| A | HOH809 |
| B | ARG106 |
| B | HOH761 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 452 |
| Chain | Residue |
| B | ARG104 |
| B | ARG105 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 453 |
| Chain | Residue |
| B | ARG181 |
| B | ARG284 |
| B | HOH775 |
| B | GLN179 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 454 |
| Chain | Residue |
| A | HOH771 |
| B | ARG299 |
| B | ARG300 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 455 |
| Chain | Residue |
| A | ARG104 |
| A | ARG105 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PA5 A 600 |
| Chain | Residue |
| A | MET45 |
| A | GLY46 |
| A | GLY47 |
| A | SER48 |
| A | SER87 |
| A | TYR88 |
| A | SER89 |
| A | THR92 |
| A | PRO134 |
| A | ARG135 |
| A | GLU203 |
| A | LYS298 |
| A | HOH601 |
| A | HOH617 |
| A | HOH705 |
| B | HIS219 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PA5 B 601 |
| Chain | Residue |
| A | HIS219 |
| B | MET45 |
| B | GLY46 |
| B | GLY47 |
| B | SER48 |
| B | SER87 |
| B | TYR88 |
| B | SER89 |
| B | THR92 |
| B | PRO134 |
| B | ARG135 |
| B | GLU203 |
| B | LYS298 |
| B | HOH608 |
| B | HOH622 |
| B | HOH645 |
| B | HOH648 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 501 |
| Chain | Residue |
| A | THR233 |
| A | GLN242 |
| A | HOH708 |
| A | HOH811 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 502 |
| Chain | Residue |
| A | PHE75 |
| A | LYS77 |
| B | SER59 |
| B | LEU60 |
| B | ASN63 |
| B | HOH806 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 266 |
| Details | Domain: {"description":"SIS","evidences":[{"source":"PROSITE-ProRule","id":"PRU00797","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"15252053","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15518558","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"15252053","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15518558","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15518558","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1X9I","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1x9h |
| Chain | Residue | Details |
| A | ARG135 | |
| A | LYS298 | |
| A | HIS219 | |
| A | GLU203 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1x9h |
| Chain | Residue | Details |
| B | ARG135 | |
| B | LYS298 | |
| B | HIS219 | |
| B | GLU203 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 736 |
| Chain | Residue | Details |
| A | ARG135 | electrostatic stabiliser |
| A | GLU203 | proton acceptor, proton donor |
| A | HIS219 | proton acceptor, proton donor |
| A | LYS298 | proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 736 |
| Chain | Residue | Details |
| B | ARG135 | electrostatic stabiliser |
| B | GLU203 | proton acceptor, proton donor |
| B | HIS219 | proton acceptor, proton donor |
| B | LYS298 | proton acceptor, proton donor |
