Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004713 | molecular_function | protein tyrosine kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
B | 0004672 | molecular_function | protein kinase activity |
B | 0004713 | molecular_function | protein tyrosine kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | binding site for residue PVB A 601 |
Chain | Residue |
A | LEU248 |
A | GLY321 |
A | ASN322 |
A | LEU370 |
A | PHE382 |
A | HOH710 |
A | HOH798 |
A | HOH808 |
A | GLY250 |
A | ALA269 |
A | VAL299 |
A | THR315 |
A | GLU316 |
A | PHE317 |
A | MET318 |
A | THR319 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue SO4 A 602 |
Chain | Residue |
A | LYS245 |
A | HIS246 |
A | LYS247 |
A | HOH702 |
A | HOH725 |
B | GLN477 |
B | HOH703 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue PVB B 601 |
Chain | Residue |
B | LEU248 |
B | ALA269 |
B | THR315 |
B | GLU316 |
B | PHE317 |
B | MET318 |
B | THR319 |
B | GLY321 |
B | LEU370 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue SO4 B 602 |
Chain | Residue |
B | ARG362 |
B | PHE393 |
B | ALA395 |
B | HIS396 |
B | HOH714 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue SO4 B 603 |
Chain | Residue |
B | ARG460 |
B | GLU462 |
B | GLY463 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGGGQYGEVYeGvwkkyslt..........VAVK |
Chain | Residue | Details |
A | LEU248-LYS271 | |
site_id | PS00109 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FIHrDLAARNCLV |
Chain | Residue | Details |
A | PHE359-VAL371 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 251 |
Details | Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | Motif: {"description":"Kinase activation loop"} |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 22 |
Details | Binding site: {} |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases","evidences":[{"source":"PubMed","id":"16912036","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00520","evidenceCode":"ECO:0000250"}]} |