Structure of PDB 2iws Chain A

Receptor sequence
>2iwsA (length=210) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
MASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSL
SDPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIGTKA
FMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWESNAG
GSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFVAY
PIQLVVTKEV
3D structure
PDB2iws Inhibition of Hsp90 with Synthetic Macrolactones: Synthesis and Structural and Biological Evaluation of Ring and Conformational Analogs of Radicicol.
ChainA
Resolution2.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 NP4 A N37 A41 D79 I82 M84 F124 T171 V213 N37 A41 D79 I82 M84 F121 T168 V210 PDBbind-CN: -logKd/Ki=6.36,Kd=0.44uM
BindingDB: IC50=5.0e+2nM
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

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Molecular Function
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Biological Process
External links
PDB RCSB:2iws, PDBe:2iws, PDBj:2iws
PDBsum2iws
PubMed17114002
UniProtP02829|HSP82_YEAST ATP-dependent molecular chaperone HSP82 (Gene Name=HSP82)

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