Structure of PDB 2vw5 Chain C

Receptor sequence
>2vw5C (length=214) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
MASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSL
SDPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSG
TKAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWES
NAGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEF
VAYPIQLVVTKEVE
3D structure
PDB2vw5 Optimizing Natural Products by Biosynthetic Engineering: Discovery of Nonquinone Hsp90 Inhibitors.
ChainC
Resolution1.9 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 BC6 C N37 D40 A41 K44 D79 M84 N92 G121 V122 F124 N37 D40 A41 K44 D79 M84 N92 G121 V122 F124 MOAD: Kd=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:2vw5, PDBe:2vw5, PDBj:2vw5
PDBsum2vw5
PubMed18800759
UniProtP02829|HSP82_YEAST ATP-dependent molecular chaperone HSP82 (Gene Name=HSP82)

[Back to BioLiP]