Structure of PDB 5vyy Chain A Binding Site BS01

Receptor Information
>5vyy 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 ID9QY
InChIInChI=1S/C20H19ClN2O4/c1-27-20(26)18-14(19(21)16(25)11-15(18)24)7-8-17-22-9-10-23(17)12-13-5-3-2-4-6-13/h2-6,9-11,24-25H,7-8,12H2,1H3
InChIKeyNCWIQXPFJORNJP-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.6COC(=O)c1c(cc(c(c1CCc2nccn2Cc3ccccc3)Cl)O)O
CACTVS 3.385COC(=O)c1c(O)cc(O)c(Cl)c1CCc2nccn2Cc3ccccc3
ACDLabs 12.01COC(=O)c3c(cc(c(c3CCc2nccn2Cc1ccccc1)Cl)O)O
FormulaC20 H19 Cl N2 O4
Namemethyl 2-[2-(1-benzyl-1H-imidazol-2-yl)ethyl]-3-chloro-4,6-dihydroxybenzoate;
resorcinylic inhibitor BnIm
ChEMBLCHEMBL3426787
DrugBank
ZINCZINC000201654561
PDB chain5vyy Chain A Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB5vyy Structure Based Design of a Grp94-Selective Inhibitor: Exploiting a Key Residue in Grp94 To Optimize Paralog-Selective Binding.
Resolution1.792 Å
Binding residue
(original residue number in PDB)		N51 D93 M98 N106 L107 F138 W162 T184
Binding residue
(residue number reindexed from 1)		N36 D78 M83 N91 L92 F123 W147 T169
Annotation score1
Binding affinityMOAD: Kd=0.62uM
PDBbind-CN: -logKd/Ki=6.21,Kd=0.62uM
BindingDB: Kd=620nM,IC50=13200nM,Ki=1800nM
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:5vyy, PDBe:5vyy, PDBj:5vyy
PDBsum5vyy
PubMed29528635
UniProtP07900|HS90A_HUMAN Heat shock protein HSP 90-alpha (Gene Name=HSP90AA1)

[Back to BioLiP]