Structure of PDB 2weq Chain A

Receptor sequence
>2weqA (length=213) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
ASETFEFQAEITQLMSLIINTVYSNKEIFLREIVSNASDALDKIRYKSLS
DPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSGT
KAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWESN
AGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFV
AYPIQLVVTKEVE
3D structure
PDB2weq Structural Basis of the Radicicol Resistance Displayed by a Fungal Hsp90
ChainA
Resolution2.2 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 GDM A N37 D40 A41 K44 E88 N92 L93 K98 G121 V122 F124 N36 D39 A40 K43 E87 N91 L92 K97 G120 V121 F123 MOAD: Kd=1.27uM
PDBbind-CN: -logKd/Ki=5.90,Kd=1.27uM
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:2weq, PDBe:2weq, PDBj:2weq
PDBsum2weq
PubMed19236053
UniProtP02829|HSP82_YEAST ATP-dependent molecular chaperone HSP82 (Gene Name=HSP82)

[Back to BioLiP]