2UV2
Crystal Structure Of Human Ste20-Like Kinase Bound To 4-(4-(5- Cyclopropyl-1H-pyrazol-3-ylamino)-quinazolin-2-ylamino)-phenyl)- acetonitrile
Replaces: 2JA0Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SCN A 1314 |
| Chain | Residue |
| A | ARG242 |
| A | LEU245 |
| A | LYS249 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SCN A 1315 |
| Chain | Residue |
| A | LYS63 |
| A | VAL92 |
| A | ILE108 |
| A | ASP173 |
| A | GVD1316 |
| A | HOH2024 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 1309 |
| Chain | Residue |
| A | HIS147 |
| A | PRO211 |
| A | TYR214 |
| A | VAL218 |
| A | THR282 |
| A | THR283 |
| A | EDO1311 |
| A | HOH2144 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 1310 |
| Chain | Residue |
| A | VAL134 |
| A | LYS137 |
| A | GLN138 |
| A | VAL294 |
| A | ASP295 |
| A | SER296 |
| A | ASN297 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 1311 |
| Chain | Residue |
| A | HIS147 |
| A | LYS150 |
| A | ASP209 |
| A | EDO1309 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 1312 |
| Chain | Residue |
| A | ASN90 |
| A | ASP168 |
| A | HOH2055 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 1313 |
| Chain | Residue |
| A | ASP27 |
| A | GLN133 |
| A | PRO290 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GVD A 1316 |
| Chain | Residue |
| A | LEU40 |
| A | ALA61 |
| A | GLU109 |
| A | CYS111 |
| A | ALA112 |
| A | LEU162 |
| A | SCN1315 |
| A | HOH2148 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGDGAFGKVYkAqnketsvl..........AAAK |
| Chain | Residue | Details |
| A | LEU40-LYS63 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKagNILF |
| Chain | Residue | Details |
| A | ILE151-PHE163 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| 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 | 1 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"O54988","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP155 | |
| A | GLY159 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP155 | |
| A | LYS157 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP155 | |
| A | THR193 | |
| A | LYS157 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP155 | |
| A | ASN160 | |
| A | LYS157 |
