Structure of PDB 2iwu Chain A

Receptor sequence
>2iwuA (length=214) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
MASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSL
SDPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSG
TKAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWES
NAGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEF
VAYPIQLVVTKEVE
3D structure
PDB2iwu Inhibition of Hsp90 with Synthetic Macrolactones: Synthesis and Structural and Biological Evaluation of Ring and Conformational Analogs of Radicicol.
ChainA
Resolution2.8 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 NP5 A N37 D79 M84 F124 T171 N37 D79 M84 F124 T171 PDBbind-CN: -logKd/Ki=5.92,Kd=1.2uM
BindingDB: IC50=3.5e+3nM
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:2iwu, PDBe:2iwu, PDBj:2iwu
PDBsum2iwu
PubMed17114002
UniProtP02829|HSP82_YEAST ATP-dependent molecular chaperone HSP82 (Gene Name=HSP82)

[Back to BioLiP]