Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004111 | molecular_function | creatine kinase activity |
A | 0004672 | molecular_function | protein kinase activity |
A | 0005524 | molecular_function | ATP binding |
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 | 0003824 | molecular_function | catalytic activity |
B | 0004111 | molecular_function | creatine kinase activity |
B | 0004672 | molecular_function | protein kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0016301 | molecular_function | kinase activity |
B | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
B | 0016775 | molecular_function | phosphotransferase activity, nitrogenous group as acceptor |
B | 0046314 | biological_process | phosphocreatine biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | binding site for residue RPI A 401 |
Chain | Residue |
A | VAL283 |
A | HOH566 |
A | HOH590 |
B | GLN266 |
B | HOH591 |
A | ASP285 |
A | SER286 |
A | GLU336 |
A | ARG338 |
A | ASP339 |
A | ARG342 |
A | EDO406 |
A | HOH531 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue EDO A 402 |
Chain | Residue |
A | ALA279 |
A | ARG282 |
A | ARG347 |
A | ARG351 |
A | HOH576 |
A | HOH587 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue EDO A 403 |
Chain | Residue |
A | ALA10 |
A | VAL11 |
A | SER12 |
A | MET15 |
A | LYS91 |
A | LEU93 |
A | GLU113 |
A | LEU130 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue EDO A 405 |
Chain | Residue |
A | ALA137 |
A | ALA239 |
A | HOH512 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue EDO A 406 |
Chain | Residue |
A | GLU336 |
A | RPI401 |
site_id | AC6 |
Number of Residues | 10 |
Details | binding site for residue RPI B 401 |
Chain | Residue |
B | ASP285 |
B | SER286 |
B | PRO322 |
B | PRO335 |
B | ARG338 |
B | ASP339 |
B | ARG342 |
B | HOH507 |
B | HOH511 |
B | HOH521 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue EDO B 402 |
Chain | Residue |
B | PHE272 |
B | TYR275 |
B | ASN307 |
B | HOH610 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue EDO B 403 |
Chain | Residue |
B | ARG86 |
B | GLU213 |
B | GLN321 |
B | PRO322 |
B | GLY323 |
B | PHE324 |
site_id | AC9 |
Number of Residues | 2 |
Details | binding site for residue EDO B 404 |
Chain | Residue |
B | PHE61 |
B | TRP149 |
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 | CYS168-THR174 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | SER27 | |
A | ARG126 | |
B | SER27 | |
B | ARG126 | |
Chain | Residue | Details |
A | HIS92 | |
A | ARG208 | |
B | HIS92 | |
B | ARG208 | |
Chain | Residue | Details |
A | ARG177 | |
B | ARG177 | |