3OT8
X-ray crystal structure of compound 17r bound to human Chk1 kinase domain
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE MI5 A 1 |
Chain | Residue |
A | ALA36 |
A | GLU134 |
A | LEU137 |
A | ASP148 |
A | HOH347 |
A | HOH401 |
A | VAL68 |
A | LEU84 |
A | GLU85 |
A | TYR86 |
A | CYS87 |
A | SER88 |
A | GLY90 |
A | GLU91 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 275 |
Chain | Residue |
A | PRO105 |
A | GLN108 |
A | ARG109 |
A | LYS267 |
A | PRO268 |
A | LEU269 |
A | HOH379 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 276 |
Chain | Residue |
A | TRP221 |
A | HIS243 |
A | LEU246 |
A | HOH345 |
A | HOH346 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 277 |
Chain | Residue |
A | ARG29 |
A | GLU32 |
A | ARG181 |
A | ASN249 |
A | HOH434 |
A | HOH459 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAYGEVQlAvnrvteea..........VAVK |
Chain | Residue | Details |
A | LEU15-LYS38 |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ItHrDIKpeNLLL |
Chain | Residue | Details |
A | ILE126-LEU138 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton acceptor"} |
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 | 2 |
Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"32357935","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |