Structure of PDB 6ceo Chain A Binding Site BS01

Receptor Information
>6ceo Chain A (length=210) 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
YPITLFVEKE
Ligand information
Ligand IDD57
InChIInChI=1S/C22H22N2O6/c1-29-21(27)19-15(20(22(28)30-2)17(26)12-16(19)25)8-9-18-23-10-11-24(18)13-14-6-4-3-5-7-14/h3-7,10-12,25-26H,8-9,13H2,1-2H3
InChIKeyRQHNBYGWOOLLIS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.385COC(=O)c1c(O)cc(O)c(C(=O)OC)c1CCc2nccn2Cc3ccccc3
OpenEye OEToolkits 2.0.6COC(=O)c1c(cc(c(c1CCc2nccn2Cc3ccccc3)C(=O)OC)O)O
ACDLabs 12.01COC(c1c(O)cc(O)c(C(=O)OC)c1CCc2nccn2Cc3ccccc3)=O
FormulaC22 H22 N2 O6
Namedimethyl 2-[2-(1-benzyl-1H-imidazol-2-yl)ethyl]-4,6-dihydroxybenzene-1,3-dicarboxylate
ChEMBLCHEMBL4098757
DrugBank
ZINC
PDB chain6ceo 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]
PDB6ceo Structure Based Design of a Grp94-Selective Inhibitor: Exploiting a Key Residue in Grp94 To Optimize Paralog-Selective Binding.
Resolution1.896 Å
Binding residue
(original residue number in PDB)		N51 D54 A55 K58 D93 G97 M98 L107 T109 F138 T184
Binding residue
(residue number reindexed from 1)		N36 D39 A40 K43 D78 G82 M83 L92 T94 F123 T169
Annotation score1
Binding affinityBindingDB: Ki=>13000nM,IC50=>100000nM
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:6ceo, PDBe:6ceo, PDBj:6ceo
PDBsum6ceo
PubMed29528635
UniProtP07900|HS90A_HUMAN Heat shock protein HSP 90-alpha (Gene Name=HSP90AA1)

[Back to BioLiP]