Structure of PDB 2xdu Chain A

Receptor sequence
>2xduA (length=208) Species: 9606 (Homo sapiens) [Search protein sequence]
VETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTD
PSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTK
AFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSA
GGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGY
PITLFVEK
3D structure
PDB2xdu Fragment-Based Drug Discovery Applied to Hsp90. Discovery of Two Lead Series with High Ligand Efficiency.
ChainA
Resolution1.74 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 MG A F22 Q23 F6 Q7
BS02 LGA A A55 M98 A39 M82 BindingDB: Kd=19000000nM
BS03 MT0 A M98 L107 F138 Y139 W162 M82 L91 F122 Y123 W146
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:2xdu, PDBe:2xdu, PDBj:2xdu
PDBsum2xdu
PubMed20718493
UniProtP07900|HS90A_HUMAN Heat shock protein HSP 90-alpha (Gene Name=HSP90AA1)

[Back to BioLiP]