Structure of PDB 2ye9 Chain A

Receptor sequence
>2ye9A (length=208) Species: 9606 (Homo sapiens) [Search protein sequence]
EVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLT
DPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGT
KAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESS
AGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIG
YPITLFVE
3D structure
PDB2ye9 How Well Can Fragments Explore Accessed Chemical Space? a Case Study from Heat Shock Protein 90.
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 3.6.4.10: non-chaperonin molecular chaperone ATPase.
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 2D4 A N51 A55 K58 D93 I96 G97 M98 L107 T109 F138 T184 E223 N36 A40 K43 D78 I81 G82 M83 L92 T94 F123 T169 E208 PDBbind-CN: -logKd/Ki=6.22,IC50=0.6uM
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:2ye9, PDBe:2ye9, PDBj:2ye9
PDBsum2ye9
PubMed21561141
UniProtP07900|HS90A_HUMAN Heat shock protein HSP 90-alpha (Gene Name=HSP90AA1)

[Back to BioLiP]