Structure of PDB 2vci Chain A Binding Site BS01

Receptor Information
>2vci Chain A (length=208) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLT
DPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGT
KAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESS
AGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIG
YPITLFVE
Ligand information
Ligand ID2GJ
InChIInChI=1S/C26H31N3O5/c1-4-27-26(32)24-23(18-7-5-17(6-8-18)15-29-9-11-33-12-10-29)25(34-28-24)20-13-19(16(2)3)21(30)14-22(20)31/h5-8,13-14,16,30-31H,4,9-12,15H2,1-3H3,(H,27,32)
InChIKeyNDAZATDQFDPQBD-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CCNC(=O)c1c(c(on1)c2cc(c(cc2O)O)C(C)C)c3ccc(cc3)CN4CCOCC4
CACTVS 3.341CCNC(=O)c1noc(c2cc(C(C)C)c(O)cc2O)c1c3ccc(CN4CCOCC4)cc3
ACDLabs 10.04O=C(NCC)c2noc(c1cc(c(O)cc1O)C(C)C)c2c3ccc(cc3)CN4CCOCC4
FormulaC26 H31 N3 O5
Name5-[2,4-DIHYDROXY-5-(1-METHYLETHYL)PHENYL]-N-ETHYL-4-[4-(MORPHOLIN-4-YLMETHYL)PHENYL]ISOXAZOLE-3-CARBOXAMIDE
ChEMBLCHEMBL252164
DrugBank
ZINCZINC000100015656
PDB chain2vci Chain A Residue 1225 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2vci 4,5-diarylisoxazole Hsp90 chaperone inhibitors: potential therapeutic agents for the treatment of cancer.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		N51 A55 K58 D93 I96 G97 M98 L107 T109 F138 T184 E223
Binding residue
(residue number reindexed from 1)		N36 A40 K43 D78 I81 G82 M83 L92 T94 F123 T169 E208
Annotation score1
Binding affinityMOAD: ic50=0.021uM
PDBbind-CN: -logKd/Ki=7.68,IC50=21nM
BindingDB: IC50=61nM,EC50=7nM,Ki=9nM
Enzymatic activity
Enzyme Commision number 3.6.4.10: non-chaperonin molecular chaperone ATPase.
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0051082 unfolded protein binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2vci, PDBe:2vci, PDBj:2vci
PDBsum2vci
PubMed18020435
UniProtP07900|HS90A_HUMAN Heat shock protein HSP 90-alpha (Gene Name=HSP90AA1)

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