6YQ1
FOCAL ADHESION KINASE CATALYTIC DOMAIN IN COMPLEX WITH N-Methyl-N-(3-{[2-(2-oxo-1,2,3,4-tetrahydro-quinolin-6-ylamino)-5-trifluoromethyl-pyrimidin-4-ylamino]-methyl}-pyridin-2-yl)-methanesulfonamide
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 |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0004713 | molecular_function | protein tyrosine kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0004713 | molecular_function | protein tyrosine kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | binding site for residue P7N A 701 |
| Chain | Residue |
| A | ARG426 |
| A | ARG550 |
| A | ASN551 |
| A | LEU553 |
| A | GLY563 |
| A | ASP564 |
| A | LEU567 |
| A | SER568 |
| A | TYR577 |
| A | HOH827 |
| A | HOH867 |
| A | GLU430 |
| A | HOH904 |
| B | GLN624 |
| A | ALA452 |
| A | MET499 |
| A | GLU500 |
| A | LEU501 |
| A | CYS502 |
| A | THR503 |
| A | GLY505 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 702 |
| Chain | Residue |
| A | GLU416 |
| A | ILE417 |
| A | ILE490 |
| A | GLU492 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 A 703 |
| Chain | Residue |
| A | SER601 |
| A | ARG668 |
| A | HOH805 |
| A | HOH937 |
| A | HOH939 |
| A | HOH944 |
| B | SER601 |
| B | ARG668 |
| C | HOH807 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | binding site for residue P7N B 701 |
| Chain | Residue |
| A | TYR516 |
| B | ARG426 |
| B | ILE428 |
| B | GLU430 |
| B | ALA452 |
| B | MET499 |
| B | GLU500 |
| B | LEU501 |
| B | CYS502 |
| B | THR503 |
| B | GLY505 |
| B | GLU506 |
| B | ARG550 |
| B | ASN551 |
| B | LEU553 |
| B | GLY563 |
| B | ASP564 |
| B | LEU567 |
| B | SER568 |
| B | TYR577 |
| B | HOH926 |
| B | HOH955 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | binding site for residue P7N C 701 |
| Chain | Residue |
| C | ARG426 |
| C | ILE428 |
| C | GLU430 |
| C | VAL436 |
| C | ALA452 |
| C | MET499 |
| C | GLU500 |
| C | LEU501 |
| C | CYS502 |
| C | GLY505 |
| C | ARG550 |
| C | ASN551 |
| C | LEU553 |
| C | GLY563 |
| C | ASP564 |
| C | LEU567 |
| C | SER568 |
| C | HOH882 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | binding site for residue P7N D 701 |
| Chain | Residue |
| D | ARG426 |
| D | ILE428 |
| D | GLU430 |
| D | VAL436 |
| D | ALA452 |
| D | MET499 |
| D | GLU500 |
| D | LEU501 |
| D | CYS502 |
| D | GLY505 |
| D | ARG550 |
| D | ASN551 |
| D | LEU553 |
| D | GLY563 |
| D | ASP564 |
| D | LEU567 |
| D | SER568 |
| D | HOH849 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 27 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGQFGDVHqGiymspenpala.......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. HrdiaarnvlVSsndCVklgDfgLsrYMeDS |
| Chain | Residue | Details |
| A | HIS544-SER574 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12467573","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine; by RET and SRC","evidences":[{"source":"PubMed","id":"15561106","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19339212","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21454698","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine; by RET and SRC","evidences":[{"source":"PubMed","id":"12387730","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19339212","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21454698","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






