2PMC
Crystal Structure of CheY-Mg(2+) in Complex with CheZ(C15) Peptide solved from a P1 Crystal
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000156 | molecular_function | phosphorelay response regulator activity |
| A | 0000160 | biological_process | phosphorelay signal transduction system |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| B | 0000156 | molecular_function | phosphorelay response regulator activity |
| B | 0000160 | biological_process | phosphorelay signal transduction system |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| C | 0000156 | molecular_function | phosphorelay response regulator activity |
| C | 0000160 | biological_process | phosphorelay signal transduction system |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| D | 0000156 | molecular_function | phosphorelay response regulator activity |
| D | 0000160 | biological_process | phosphorelay signal transduction system |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 201 |
| Chain | Residue |
| A | ASP13 |
| A | ASP57 |
| A | ASN59 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 202 |
| Chain | Residue |
| B | ASP13 |
| B | ASP57 |
| B | ASN59 |
| B | HOH206 |
| B | HOH207 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 468 |
| Details | Domain: {"description":"Response regulatory","evidences":[{"source":"PROSITE-ProRule","id":"PRU00169","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"A0A0H3AMJ9","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16674976","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18083806","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8257674","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2CHE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FKA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FLW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FMH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FMK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PL9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PMC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"4-aspartylphosphate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00169","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1902474","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3280143","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
