Structure of PDB 1bgq Chain A

Receptor sequence
>1bgqA (length=214) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
MASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSL
SDPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSG
TKAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWES
NAGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEF
VAYPIQLVVTKEVE
3D structure
PDB1bgq Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin.
ChainA
Resolution2.5 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 RDC A N37 D40 K44 D79 M84 F124 L173 N37 D40 K44 D79 M84 F124 L173 MOAD: Kd=2.7nM
PDBbind-CN: -logKd/Ki=8.57,Kd=2.7nM
BindingDB: IC50=2e+2nM
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:1bgq, PDBe:1bgq, PDBj:1bgq
PDBsum1bgq
PubMed9925731
UniProtP02829|HSP82_YEAST ATP-dependent molecular chaperone HSP82 (Gene Name=HSP82)

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