5VIL
Crystal structure of ASK1 kinase domain with a potent inhibitor (analog 6)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| D | 0004672 | molecular_function | protein 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 | 19 |
| Details | binding site for residue 9E1 A 1001 |
| Chain | Residue |
| A | LEU686 |
| A | VAL757 |
| A | PRO758 |
| A | GLY759 |
| A | GLY760 |
| A | ASP807 |
| A | LEU810 |
| A | SER821 |
| A | ASP822 |
| A | DMS1002 |
| B | TYR814 |
| A | LYS688 |
| A | GLY689 |
| A | ALA707 |
| A | LYS709 |
| A | VAL738 |
| A | MET754 |
| A | GLU755 |
| A | GLN756 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue DMS A 1002 |
| Chain | Residue |
| A | TYR814 |
| A | 9E11001 |
| B | TYR814 |
| B | DMS1004 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | binding site for residue 9E1 B 1001 |
| Chain | Residue |
| A | TYR814 |
| B | LEU686 |
| B | GLY689 |
| B | ALA707 |
| B | LYS709 |
| B | VAL738 |
| B | GLU755 |
| B | GLN756 |
| B | VAL757 |
| B | PRO758 |
| B | GLY759 |
| B | GLY760 |
| B | ASP807 |
| B | ASN808 |
| B | LEU810 |
| B | SER821 |
| B | ASP822 |
| B | DMS1004 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue DMS B 1002 |
| Chain | Residue |
| A | GLU676 |
| A | GLN703 |
| B | LYS769 |
| B | TRP770 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue DMS B 1003 |
| Chain | Residue |
| A | LYS769 |
| A | TRP770 |
| B | GLU676 |
| B | ARG698 |
| B | GLN703 |
| B | ARG705 |
| B | HOH1108 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue DMS B 1004 |
| Chain | Residue |
| A | DMS1002 |
| B | TYR814 |
| B | 9E11001 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | binding site for residue 9E1 C 4000 |
| Chain | Residue |
| C | LEU686 |
| C | GLY689 |
| C | ALA707 |
| C | LYS709 |
| C | VAL738 |
| C | MET754 |
| C | GLU755 |
| C | GLN756 |
| C | VAL757 |
| C | PRO758 |
| C | GLY759 |
| C | GLY760 |
| C | ASP807 |
| C | ASN808 |
| C | LEU810 |
| C | ASP822 |
| D | TYR814 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | binding site for residue 9E1 D 4000 |
| Chain | Residue |
| C | TYR814 |
| D | LEU686 |
| D | ALA707 |
| D | LYS709 |
| D | VAL738 |
| D | MET754 |
| D | GLU755 |
| D | GLN756 |
| D | VAL757 |
| D | PRO758 |
| D | GLY759 |
| D | GLY760 |
| D | ASP807 |
| D | LEU810 |
| D | ASP822 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGTYGIVYaGrdlsnqvr..........IAIK |
| Chain | Residue | Details |
| A | LEU686-LYS709 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDIKgdNVLI |
| Chain | Residue | Details |
| A | ILE799-ILE811 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1032 |
| Details | Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"16407264","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"17937911","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis, MELK and MAP3K6","evidences":[{"source":"PubMed","id":"11920685","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17210579","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17937911","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18948261","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19590015","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23102700","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
