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 | 0016310 | biological_process | phosphorylation |
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 | 0016310 | biological_process | phosphorylation |
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 | 5 |
Details | binding site for residue FMT A 401 |
Chain | Residue |
A | SER27 |
A | ARG29 |
A | SER179 |
A | MET181 |
A | HOH535 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue FMT A 402 |
Chain | Residue |
A | GLU122 |
A | CYS168 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue EDO A 403 |
Chain | Residue |
A | GLU122 |
A | ARG126 |
A | ARG177 |
A | HOH502 |
A | HOH507 |
A | ARG29 |
A | ARG31 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue EDO A 404 |
Chain | Residue |
A | THR9 |
A | ALA10 |
A | VAL11 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue EDO A 405 |
Chain | Residue |
A | LYS270 |
A | SER274 |
A | ILE277 |
A | CYS292 |
A | HOH539 |
A | HOH546 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue EDO A 406 |
Chain | Residue |
A | ALA50 |
A | PRO103 |
A | PHE104 |
A | GLY105 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue EDO A 407 |
Chain | Residue |
A | SER144 |
A | ASP147 |
A | GLU234 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue EDO A 408 |
Chain | Residue |
A | VAL89 |
A | GLU90 |
A | HIS92 |
A | TYR211 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue EDO A 409 |
Chain | Residue |
A | ARG208 |
A | GLY209 |
A | THR210 |
A | TYR211 |
A | GLY212 |
A | GLY214 |
A | GLU216 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue EDO A 410 |
Chain | Residue |
A | VAL11 |
A | SER12 |
A | MET15 |
A | LEU93 |
A | GLU113 |
A | HOH581 |
site_id | AD2 |
Number of Residues | 1 |
Details | binding site for residue EDO A 411 |
site_id | AD3 |
Number of Residues | 2 |
Details | binding site for residue EDO A 412 |
site_id | AD4 |
Number of Residues | 2 |
Details | binding site for residue EDO A 413 |
Chain | Residue |
A | GLN17 |
A | GLN135 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue EDO A 414 |
Chain | Residue |
A | HIS92 |
A | MET181 |
A | TYR211 |
A | ASN314 |
A | ILE318 |
site_id | AD6 |
Number of Residues | 6 |
Details | binding site for residue EDO A 415 |
Chain | Residue |
A | TYR66 |
A | GLY67 |
A | GLU68 |
A | ALA69 |
A | HOH515 |
A | HOH660 |
site_id | AD7 |
Number of Residues | 3 |
Details | binding site for residue EDO A 416 |
Chain | Residue |
A | HOH514 |
A | HOH601 |
A | HOH627 |
site_id | AD8 |
Number of Residues | 5 |
Details | binding site for residue EDO A 417 |
Chain | Residue |
A | ALA137 |
A | LEU140 |
A | GLU141 |
A | HOH503 |
A | HOH573 |
site_id | AD9 |
Number of Residues | 2 |
Details | binding site for residue IMD A 418 |
Chain | Residue |
A | GLU151 |
A | TYR164 |
site_id | AE1 |
Number of Residues | 5 |
Details | binding site for residue EDO B 401 |
Chain | Residue |
B | SER286 |
B | MET317 |
B | THR320 |
B | GLN321 |
B | HOH570 |
site_id | AE2 |
Number of Residues | 3 |
Details | binding site for residue EDO B 402 |
Chain | Residue |
B | HIS92 |
B | TYR211 |
B | ASN314 |
site_id | AE3 |
Number of Residues | 5 |
Details | binding site for residue IMD B 403 |
Chain | Residue |
B | SER27 |
B | ARG29 |
B | LEU130 |
B | SER179 |
B | MET181 |
site_id | AE4 |
Number of Residues | 2 |
Details | binding site for residue IMD B 404 |
Chain | Residue |
B | LEU319 |
B | PHE324 |
site_id | AE5 |
Number of Residues | 2 |
Details | binding site for residue IMD B 405 |
Chain | Residue |
B | SER144 |
B | ASP147 |
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 | |