1I0E
CRYSTAL STRUCTURE OF CREATINE KINASE FROM HUMAN MUSCLE
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
A | 0046314 | biological_process | phosphocreatine biosynthetic process |
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 | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
B | 0046314 | biological_process | phosphocreatine biosynthetic process |
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 | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
C | 0046314 | biological_process | phosphocreatine biosynthetic process |
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 | 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 | 24 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00843 |
Chain | Residue | Details |
A | SER128 | |
B | ARG292 | |
B | ARG320 | |
B | ASP335 | |
C | SER128 | |
C | HIS191 | |
C | ARG236 | |
C | ARG292 | |
C | ARG320 | |
C | ASP335 | |
D | SER128 | |
A | HIS191 | |
D | HIS191 | |
D | ARG236 | |
D | ARG292 | |
D | ARG320 | |
D | ASP335 | |
A | ARG236 | |
A | ARG292 | |
A | ARG320 | |
A | ASP335 | |
B | SER128 | |
B | HIS191 | |
B | ARG236 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07310 |
Chain | Residue | Details |
A | SER164 | |
D | SER164 | |
D | SER199 | |
D | SER372 | |
A | SER199 | |
A | SER372 | |
B | SER164 | |
B | SER199 | |
B | SER372 | |
C | SER164 | |
C | SER199 | |
C | SER372 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P00564 |
Chain | Residue | Details |
A | THR166 | |
D | THR166 | |
D | THR180 | |
D | THR313 | |
A | THR180 | |
A | THR313 | |
B | THR166 | |
B | THR180 | |
B | THR313 | |
C | THR166 | |
C | THR180 | |
C | THR313 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00564 |
Chain | Residue | Details |
A | SER178 | |
B | SER178 | |
C | SER178 | |
D | SER178 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P07310 |
Chain | Residue | Details |
A | THR322 | |
B | THR322 | |
C | THR322 | |
D | THR322 |
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 |