8WTC
Crystal structure of McsB kinase domain complexed with McsA.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004111 | molecular_function | creatine kinase activity |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| A | 0016775 | molecular_function | phosphotransferase activity, nitrogenous group as acceptor |
| A | 0046314 | biological_process | phosphocreatine biosynthetic process |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0006508 | biological_process | proteolysis |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0046870 | molecular_function | cadmium ion binding |
| B | 0050897 | molecular_function | cobalt ion binding |
| B | 1990169 | biological_process | stress response to copper ion |
| B | 1990170 | biological_process | stress response to cadmium ion |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004111 | molecular_function | creatine kinase activity |
| C | 0016301 | molecular_function | kinase activity |
| C | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| C | 0016775 | molecular_function | phosphotransferase activity, nitrogenous group as acceptor |
| C | 0046314 | biological_process | phosphocreatine biosynthetic process |
| D | 0005507 | molecular_function | copper ion binding |
| D | 0006508 | biological_process | proteolysis |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0046870 | molecular_function | cadmium ion binding |
| D | 0050897 | molecular_function | cobalt ion binding |
| D | 1990169 | biological_process | stress response to copper ion |
| D | 1990170 | biological_process | stress response to cadmium ion |
Functional Information from PROSITE/UniProt
| site_id | PS00112 |
| Number of Residues | 7 |
| Details | PHOSPHAGEN_KINASE Phosphagen kinase active site signature. CP.TNVGT |
| Chain | Residue | Details |
| A | CYS167-THR173 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00602","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoarginine; by autocatalysis","evidences":[{"source":"PubMed","id":"21622759","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoarginine; by autocatalysis","evidences":[{"source":"PubMed","id":"24263382","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoarginine; by autocatalysis","evidences":[{"source":"PubMed","id":"21622759","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24263382","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 70 |
| Details | Domain: {"description":"UVR","evidences":[{"source":"PROSITE-ProRule","id":"PRU00217","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoarginine","evidences":[{"source":"PubMed","id":"24263382","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoarginine","evidences":[{"source":"PubMed","id":"22517742","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
