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 | 2 |
| Details | binding site for residue MG A 701 |
| Chain | Residue |
| A | ASP564 |
| A | ANP702 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | binding site for residue ANP A 702 |
| Chain | Residue |
| A | LEU501 |
| A | CYS502 |
| A | GLU506 |
| A | ARG550 |
| A | ASN551 |
| A | LEU553 |
| A | ASP564 |
| A | MG701 |
| A | GLY429 |
| A | GLU430 |
| A | GLY431 |
| A | GLN432 |
| A | VAL436 |
| A | LYS454 |
| A | GLU500 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue MG B 701 |
| Chain | Residue |
| B | ASP564 |
| B | ANP702 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue ANP B 702 |
| Chain | Residue |
| B | GLY429 |
| B | GLU430 |
| B | GLY431 |
| B | GLN432 |
| B | VAL436 |
| B | LYS454 |
| B | GLU500 |
| B | LEU501 |
| B | CYS502 |
| B | GLU506 |
| B | ARG550 |
| B | ASN551 |
| B | LEU553 |
| B | ASP564 |
| B | MG701 |
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 | 516 |
| Details | Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| 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 | 18 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"12370821","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"source":"PubMed","id":"12370821","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17574028","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"evidenceCode":"ECO:0000250"}]} |
