Structure of PDB 2yge Chain A

Receptor sequence
>2ygeA (length=214) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
MASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDRIRYKSL
SDPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIANSG
TKAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWES
NAGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEF
VAYPIQLVVTKEVE
3D structure
PDB2yge 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
Resolution1.956 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 D79 M84 N92 N98 G121 V122 F124 N37 D40 A41 D79 M84 N92 N98 G121 V122 F124 MOAD: Kd=8.62uM
PDBbind-CN: -logKd/Ki=5.06,Kd=8.62uM
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:2yge, PDBe:2yge, PDBj:2yge
PDBsum2yge
PubMed21778327
UniProtP02829|HSP82_YEAST ATP-dependent molecular chaperone HSP82 (Gene Name=HSP82)

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