Structure of PDB 2xx2 Chain D

Receptor sequence
>2xx2D (length=214) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
MASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSL
SDPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSG
TKAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWES
NAGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEF
VAYPIQLVVTKEVE
3D structure
PDB2xx2 Targeting the Hsp90 Molecular Chaperone with Novel Macrolactams. Synthesis, Structural, Binding, and Cellular Studies.
ChainD
Resolution1.85 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 13C D N37 A41 K44 D79 I82 M84 N92 F124 T171 L173 N37 A41 K44 D79 I82 M84 N92 F124 T171 L173
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:2xx2, PDBe:2xx2, PDBj:2xx2
PDBsum2xx2
PubMed21932796
UniProtP02829|HSP82_YEAST ATP-dependent molecular chaperone HSP82 (Gene Name=HSP82)

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