4BID
Crystal Structures of Ask1-inhibitor Complexes
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE IE8 A 4000 |
| Chain | Residue |
| A | LEU686 |
| A | VAL757 |
| A | ASP807 |
| A | ASN808 |
| A | LEU810 |
| A | ASP822 |
| A | GLY687 |
| A | ALA707 |
| A | LYS709 |
| A | VAL738 |
| A | ILE752 |
| A | MET754 |
| A | GLU755 |
| A | GLN756 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE IE8 B 4000 |
| Chain | Residue |
| B | LEU686 |
| B | GLY687 |
| B | LYS688 |
| B | ALA707 |
| B | LYS709 |
| B | VAL738 |
| B | ILE752 |
| B | MET754 |
| B | GLU755 |
| B | GLN756 |
| B | VAL757 |
| B | ASP807 |
| B | LEU810 |
| B | ASP822 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT A 1940 |
| Chain | Residue |
| A | GLU676 |
| A | GLN703 |
| A | LYS769 |
| A | TRP770 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B 1941 |
| Chain | Residue |
| B | GLU676 |
| B | GLN703 |
| B | ARG705 |
| B | LYS769 |
| B | TRP770 |
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 | 2 |
| 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_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"17937911","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| 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 |
