1XDP
Crystal Structure of the E.coli Polyphosphate Kinase in complex with AMPPNP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006799 | biological_process | polyphosphate biosynthetic process |
| A | 0008976 | molecular_function | polyphosphate kinase activity |
| A | 0009358 | cellular_component | polyphosphate kinase complex |
| A | 0016020 | cellular_component | membrane |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016776 | molecular_function | phosphotransferase activity, phosphate group as acceptor |
| A | 0016778 | molecular_function | diphosphotransferase activity |
| A | 0031241 | cellular_component | periplasmic side of cell outer membrane |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0043751 | molecular_function | polyphosphate:AMP phosphotransferase activity |
| A | 0046777 | biological_process | protein autophosphorylation |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051302 | biological_process | regulation of cell division |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006799 | biological_process | polyphosphate biosynthetic process |
| B | 0008976 | molecular_function | polyphosphate kinase activity |
| B | 0009358 | cellular_component | polyphosphate kinase complex |
| B | 0016020 | cellular_component | membrane |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016776 | molecular_function | phosphotransferase activity, phosphate group as acceptor |
| B | 0016778 | molecular_function | diphosphotransferase activity |
| B | 0031241 | cellular_component | periplasmic side of cell outer membrane |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0043751 | molecular_function | polyphosphate:AMP phosphotransferase activity |
| B | 0046777 | biological_process | protein autophosphorylation |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051302 | biological_process | regulation of cell division |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 702 |
| Chain | Residue |
| A | ARG375 |
| A | ARG405 |
| A | ATP701 |
| A | MG703 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 703 |
| Chain | Residue |
| A | TYR374 |
| A | ARG375 |
| A | ARG405 |
| A | ATP701 |
| A | MG702 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 705 |
| Chain | Residue |
| B | ARG405 |
| B | ATP704 |
| B | MG706 |
| B | HOH743 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 706 |
| Chain | Residue |
| B | ARG53 |
| B | ARG405 |
| B | ATP704 |
| B | MG705 |
| B | HOH743 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ATP A 701 |
| Chain | Residue |
| A | PHE17 |
| A | ILE41 |
| A | ASN45 |
| A | TYR374 |
| A | ARG375 |
| A | ARG405 |
| A | HIS435 |
| A | TYR468 |
| A | ARG564 |
| A | HIS592 |
| A | MG702 |
| A | MG703 |
| A | HOH719 |
| A | HOH724 |
| A | HOH765 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ATP B 704 |
| Chain | Residue |
| B | PHE17 |
| B | VAL21 |
| B | ILE41 |
| B | ASN45 |
| B | TYR374 |
| B | ARG375 |
| B | HIS435 |
| B | TYR468 |
| B | ARG564 |
| B | ASP587 |
| B | LEU590 |
| B | HIS592 |
| B | MG705 |
| B | MG706 |
| B | HOH707 |
| B | HOH723 |
| B | HOH731 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 68 |
| Details | Domain: {"description":"PLD phosphodiesterase","evidences":[{"source":"HAMAP-Rule","id":"MF_00347","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Phosphohistidine intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_00347","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8962061","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15947782","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00347","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"1XDP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
