Structure of PDB 2ygf Chain A

Receptor sequence
>2ygfA (length=213) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
ASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLS
DPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAEVINNIGTIAKSGT
KAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQMISKSNDDEQYIWESN
AGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFV
AYPIQLVVTKEVE
3D structure
PDB2ygf Features of the Streptomyces Hygroscopicus Htpg Reveal How Partial Geldanamycin Resistance Can Arise by Mutation to the ATP Binding Pocket of a Eukaryotic Hsp90.
ChainA
Resolution2.0 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 GDM A N37 D40 A41 K44 D79 N92 K98 G121 V122 F124 N36 D39 A40 K43 D78 N91 K97 G120 V121 F123 MOAD: Kd~10uM
PDBbind-CN: -logKd/Ki=5.09,Kd=8.06uM
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:2ygf, PDBe:2ygf, PDBj:2ygf
PDBsum2ygf
PubMed21778327
UniProtP02829|HSP82_YEAST ATP-dependent molecular chaperone HSP82 (Gene Name=HSP82)

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