Structure of PDB 3b28 Chain A Binding Site BS01

Receptor Information
>3b28 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 IDB2X
InChIInChI=1S/C16H13ClN4OS/c1-23-16-20-14(19-15(18)21-16)13-10-4-2-3-8-6-22-7-9(12(8)10)5-11(13)17/h2-5H,6-7H2,1H3,(H2,18,19,20,21)
InChIKeyFPTCGMGLTQPTGE-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01Clc2c(c1cccc3c1c(c2)COC3)c4nc(nc(SC)n4)N
OpenEye OEToolkits 1.7.2CSc1nc(nc(n1)N)c2c3cccc4c3c(cc2Cl)COC4
CACTVS 3.370CSc1nc(N)nc(n1)c2c(Cl)cc3COCc4cccc2c34
FormulaC16 H13 Cl N4 O S
Name4-(5-chloro-1H,3H-benzo[de]isochromen-6-yl)-6-(methylsulfanyl)-1,3,5-triazin-2-amine
ChEMBLCHEMBL1834096
DrugBank
ZINCZINC000072126864
PDB chain3b28 Chain A Residue 237 [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]
PDB3b28 Lead generation of heat shock protein 90 inhibitors by a combination of fragment-based approach, virtual screening, and structure-based drug design
Resolution1.35 Å
Binding residue
(original residue number in PDB)		A55 G97 M98 N106 L107 F138 Y139
Binding residue
(residue number reindexed from 1)		A40 G82 M83 N91 L92 F123 Y124
Annotation score1
Binding affinityMOAD: Kd=0.0034uM
PDBbind-CN: -logKd/Ki=8.47,Kd=0.0034uM
BindingDB: Kd=3.4nM,IC50=3000nM
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:3b28, PDBe:3b28, PDBj:3b28
PDBsum3b28
PubMed21875802
UniProtP07900|HS90A_HUMAN Heat shock protein HSP 90-alpha (Gene Name=HSP90AA1)

[Back to BioLiP]