Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T94366 | Target Info | |||
| Target Name | Hsp90 co-chaperone Cdc37 (CDC37) | ||||
| Synonyms | p50Cdc37; Hsp90 co-chaperone Cdc37, N-terminally processed; Hsp90 chaperone protein kinase-targeting subunit; CDC37A | ||||
| Target Type | Literature-reported Target | ||||
| Gene Name | CDC37 | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | L-serine-O-phosphate | Ligand Info | |||
| Canonical SMILES | C(C(C(=O)O)N)OP(=O)(O)O | ||||
| InChI | 1S/C3H8NO6P/c4-2(3(5)6)1-10-11(7,8)9/h2H,1,4H2,(H,5,6)(H2,7,8,9)/t2-/m0/s1 | ||||
| InChIKey | BZQFBWGGLXLEPQ-REOHCLBHSA-N | ||||
| PubChem Compound ID | 68841 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 5FWK Atomic cryoEM structure of Hsp90-Cdc37-Cdk4 complex | ||||||
| Method | Electron microscopy | Resolution | 3.90 Å | Mutation | No | [1] |
| PDB Sequence |
VDYSVWDHIE
11 VDDEDETHPN22 IDTASLFRWR32 HQARVERMEQ42 FQKEKEELDR52 GCRECKRKVA 62 ECQRKLKELE72 VAEGGKAELE82 RLQAEAQQLR92 KEERSWEQKL102 EEMRKKEKSM 112 PWNVDTLSKD122 GFSKSMVNTK132 P
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| PDB ID: 7Z38 Structure of the RAF1-HSP90-CDC37 complex (RHC-I) | ||||||
| Method | Electron microscopy | Resolution | 3.16 Å | Mutation | No | [2] |
| PDB Sequence |
VDYSVWDHIE
11 VDDEDETHPN22 IDTASLFRWR32 HQARVERMEQ42 FQKEKEELDR52 GCRECKRKVA 62 ECQRKLKELE72 VAEGGKAELE82 RLQAEAQQLR92 KEERSWEQKL102 EEMRKKEKSM 112 PWNVDTLSKD122 GFSKSMVNTK132 PEKTEEDSEE142 VREQKHKTFV152 EKYEKQIKHF 162 GMLRRWDDSQ172 KYLSDNVHLV182 CEETANYLVI192 WCIDLEVEEK202 CALMEQVAHQ 212 TIVMQFILEL222 AKSLKVDPRA232 CFRQFFTKIK242 TADRQYMEGF252 NDELEAFKER 262 VRGRAKLRIE272 KA
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase. Science. 2016 Jun 24;352(6293):1542-7. | ||||
| REF 2 | Structure of the RAF1-HSP90-CDC37 complex reveals the basis of RAF1 regulation. Mol Cell. 2022 Sep 15;82(18):3438-3452.e8. | ||||
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