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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | binding site for residue 1N1 A 1001 |
| Chain | Residue |
| A | ILE619 |
| A | TYR694 |
| A | MET695 |
| A | GLU696 |
| A | GLY698 |
| A | LYS702 |
| A | GLU706 |
| A | LEU746 |
| A | SER756 |
| A | HOH1111 |
| A | HOH1204 |
| A | ALA644 |
| A | HOH1210 |
| A | HOH1280 |
| A | HOH1318 |
| A | ILE645 |
| A | LYS646 |
| A | GLU663 |
| A | MET667 |
| A | ILE690 |
| A | THR692 |
| A | GLU693 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 1002 |
| Chain | Residue |
| A | ASN732 |
| A | GLU815 |
| A | LYS863 |
| A | PHE864 |
| A | ALA865 |
| A | HOH1144 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 1003 |
| Chain | Residue |
| A | ILE781 |
| A | THR784 |
| A | ILE789 |
| A | MET827 |
| A | ILE830 |
| A | HOH1118 |
| A | HOH1121 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 1004 |
| Chain | Residue |
| A | HIS673 |
| A | ASN748 |
| A | ASN750 |
| A | VAL752 |
| A | LYS754 |
| A | HOH1186 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 28 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGAGEFGEVYkGmlktssgkkevp......VAIK |
| Chain | Residue | Details |
| A | ILE619-LYS646 | |
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. YVHrDLAARNILV |
| Chain | Residue | Details |
| A | TYR735-VAL747 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| 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_FI2 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"UniProtKB","id":"Q03145","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q03145","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
