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 | 12 |
| Details | BINDING SITE FOR RESIDUE 4ST A1687 |
| Chain | Residue |
| A | ILE428 |
| A | ARG550 |
| A | LEU553 |
| B | ARG426 |
| A | GLY429 |
| A | GLU430 |
| A | ALA452 |
| A | GLU500 |
| A | LEU501 |
| A | CYS502 |
| A | GLY505 |
| A | GLU506 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 4ST B1687 |
| Chain | Residue |
| A | ARG426 |
| B | ILE428 |
| B | GLY429 |
| B | ALA452 |
| B | LYS454 |
| B | VAL484 |
| B | GLU500 |
| B | LEU501 |
| B | CYS502 |
| B | GLY505 |
| B | GLU506 |
| B | ARG550 |
| B | ASN551 |
| B | LEU553 |
| B | ASP564 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 27 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGQFGDVHqGiymspenpama.......VAIK |
| Chain | Residue | Details |
| A | ILE428-LYS454 | |
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDIAARNVLV |
| Chain | Residue | Details |
| A | PHE542-VAL554 | |
| site_id | PS00661 |
| Number of Residues | 31 |
| Details | FERM_2 FERM domain signature 2. HrdiaarnvlVSatdCVklgDfgLsrYMeDS |
| Chain | Residue | Details |
| A | HIS544-SER574 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 640 |
| Details | Domain: {"description":"FERM","evidences":[{"source":"PROSITE-ProRule","id":"PRU00084","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| 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_FI3 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"12370821","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ARG550 | |
| A | ASP546 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ARG550 | |
| B | ASP546 | |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP546 | |
| A | ALA548 | |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP546 | |
| B | ALA548 | |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASN551 | |
| A | ASP546 | |
| A | ALA548 | |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASN551 | |
| B | ASP546 | |
| B | ALA548 | |
