Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004674 | molecular_function | protein serine/threonine kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
B | 0004672 | molecular_function | protein kinase activity |
B | 0004674 | molecular_function | protein serine/threonine kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006468 | biological_process | protein phosphorylation |
C | 0004672 | molecular_function | protein kinase activity |
C | 0004674 | molecular_function | protein serine/threonine kinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0006468 | biological_process | protein phosphorylation |
D | 0004672 | molecular_function | protein kinase activity |
D | 0004674 | molecular_function | protein serine/threonine kinase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE 5QM D 1334 |
Chain | Residue |
D | ALA38 |
D | GLU57 |
D | GLU87 |
D | CYS89 |
D | LEU139 |
D | ILE149 |
D | ASP150 |
D | HOH2034 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 5QM A 1334 |
Chain | Residue |
A | ALA38 |
A | GLU57 |
A | GLU87 |
A | CYS89 |
A | LEU139 |
A | ILE149 |
A | ASP150 |
A | HOH2043 |
A | ILE17 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE 5QM B 1334 |
Chain | Residue |
B | ILE17 |
B | ALA38 |
B | GLU57 |
B | GLU87 |
B | CYS89 |
B | ILE149 |
B | ASP150 |
B | HOH2043 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE 5QM C 1334 |
Chain | Residue |
C | ILE17 |
C | VAL25 |
C | ALA38 |
C | GLU57 |
C | GLU87 |
C | CYS89 |
C | LEU139 |
C | ILE149 |
C | ASP150 |
C | HOH2036 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGTGGFAKVKlAchiltgem..........VAIK |
Chain | Residue | Details |
A | ILE17-LYS40 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. YaHrDLKpeNLLF |
Chain | Residue | Details |
A | TYR128-PHE140 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 117 |
Details | Region: {"description":"UBA-like"} |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
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 | 28 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"16216881","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"16216881","evidenceCode":"ECO:0000269"}]} |