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 | 25 |
| Details | BINDING SITE FOR CHAIN C OF MACROCYCLIC INHIBITOR MC1 |
| Chain | Residue |
| A | GLY276 |
| A | TYR340 |
| A | MET341 |
| A | GLY344 |
| A | SER345 |
| A | LEU347 |
| A | ASP348 |
| A | ASP386 |
| A | ARG388 |
| A | ALA390 |
| A | ASN391 |
| A | CYS277 |
| A | LEU393 |
| A | ASP404 |
| A | PHE424 |
| A | PRO425 |
| B | SER522 |
| C | HOH102 |
| A | PHE278 |
| A | GLY279 |
| A | GLU280 |
| A | VAL281 |
| A | ALA293 |
| A | LYS295 |
| A | LEU297 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR CHAIN D OF MACROCYCLIC INHIBITOR MC1 |
| Chain | Residue |
| A | SER522 |
| B | GLY274 |
| B | GLN275 |
| B | GLY276 |
| B | PHE278 |
| B | VAL281 |
| B | ALA293 |
| B | THR296 |
| B | GLU339 |
| B | MET341 |
| B | GLY344 |
| B | LEU347 |
| B | ARG388 |
| B | ALA390 |
| B | LEU393 |
| B | HOH640 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 23 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGCFGEVWmGtwngttr...........VAIK |
| Chain | Residue | Details |
| A | LEU273-LYS295 | |
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. YVHrDLRAANILV |
| Chain | Residue | Details |
| A | TYR382-VAL394 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| 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_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"8856081","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"19948721","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine; by CSK","evidences":[{"source":"PubMed","id":"2420005","evidenceCode":"ECO:0000269"}]} |
