1I0E
CRYSTAL STRUCTURE OF CREATINE KINASE FROM HUMAN MUSCLE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004111 | molecular_function | creatine kinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| A | 0046314 | biological_process | phosphocreatine biosynthetic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004111 | molecular_function | creatine kinase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| B | 0046314 | biological_process | phosphocreatine biosynthetic process |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004111 | molecular_function | creatine kinase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005615 | cellular_component | extracellular space |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0016301 | molecular_function | kinase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| C | 0046314 | biological_process | phosphocreatine biosynthetic process |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004111 | molecular_function | creatine kinase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005615 | cellular_component | extracellular space |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0016301 | molecular_function | kinase activity |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| D | 0046314 | biological_process | phosphocreatine biosynthetic process |
Functional Information from PROSITE/UniProt
| site_id | PS00112 |
| Number of Residues | 7 |
| Details | PHOSPHAGEN_KINASE Phosphagen kinase active site signature. CP.SNLGT |
| Chain | Residue | Details |
| A | CYS283-THR289 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 348 |
| Details | Domain: {"description":"Phosphagen kinase N-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00842","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00843","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P07310","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P00564","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00564","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P07310","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1bg0 |
| Chain | Residue | Details |
| A | ARG236 | |
| A | ARG292 | |
| A | ARG320 | |
| A | ARG132 | |
| A | GLU232 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1bg0 |
| Chain | Residue | Details |
| B | ARG236 | |
| B | ARG292 | |
| B | ARG320 | |
| B | ARG132 | |
| B | GLU232 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1bg0 |
| Chain | Residue | Details |
| C | ARG236 | |
| C | ARG292 | |
| C | ARG320 | |
| C | ARG132 | |
| C | GLU232 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1bg0 |
| Chain | Residue | Details |
| D | ARG236 | |
| D | ARG292 | |
| D | ARG320 | |
| D | ARG132 | |
| D | GLU232 |
