Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
B | 0004672 | molecular_function | protein kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006468 | biological_process | protein phosphorylation |
C | 0004672 | molecular_function | protein kinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | binding site for residue 58C A 401 |
Chain | Residue |
A | VAL31 |
A | ASP115 |
A | GLN157 |
A | LEU160 |
A | VAL170 |
A | ASN33 |
A | VAL39 |
A | ALA52 |
A | MET105 |
A | GLU106 |
A | CYS108 |
A | GLY111 |
A | SER112 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 402 |
Chain | Residue |
A | ARG19 |
B | ASP211 |
B | LYS213 |
B | HIS274 |
B | SER275 |
site_id | AC3 |
Number of Residues | 12 |
Details | binding site for residue 58C B 401 |
Chain | Residue |
B | VAL31 |
B | VAL39 |
B | ALA52 |
B | MET105 |
B | GLU106 |
B | PHE107 |
B | CYS108 |
B | GLY111 |
B | ASP115 |
B | GLN157 |
B | LEU160 |
B | VAL170 |
site_id | AC4 |
Number of Residues | 11 |
Details | binding site for residue 58C C 401 |
Chain | Residue |
C | VAL31 |
C | ALA52 |
C | MET105 |
C | GLU106 |
C | CYS108 |
C | GLY111 |
C | ASP115 |
C | GLN157 |
C | LEU160 |
C | VAL170 |
C | ASP171 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue SO4 C 402 |
Chain | Residue |
B | ARG19 |
C | ASP211 |
C | LYS213 |
C | HIS274 |
C | SER275 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue SO4 C 403 |
Chain | Residue |
A | LYS213 |
A | HIS274 |
A | SER275 |
C | ARG19 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGNGTYGQVYkGrhvktgql..........AAIK |
Chain | Residue | Details |
A | VAL31-LYS54 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDIKgqNVLL |
Chain | Residue | Details |
A | VAL149-LEU161 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 57 |
Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 27 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P83510","evidenceCode":"ECO:0000250"}]} |