4GU6
FOCAL ADHESION KINASE CATALYTIC DOMAIN IN COMPLEX WITH N-{3-[(5-Cyano-2-phenyl-1H-pyrrolo[2,3-b]pyridin-4-ylamino)- methyl]-pyridin-2-yl}-N-methyl-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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 10N A 701 |
| Chain | Residue |
| A | GLU430 |
| A | LEU553 |
| A | GLY563 |
| A | ASP564 |
| A | LEU567 |
| A | SER568 |
| A | HOH1012 |
| A | ASN493 |
| A | GLU500 |
| A | LEU501 |
| A | CYS502 |
| A | THR503 |
| A | GLY505 |
| A | ARG550 |
| A | ASN551 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 10N B 701 |
| Chain | Residue |
| B | ILE428 |
| B | GLU430 |
| 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 |
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 | 2 |
| 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 | 18 |
| 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 | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| 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 | 1 |
| 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 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
