Structure of PDB 2xdu Chain A Binding Site BS03

Receptor Information

>2xdu Chain A (length=208) Species: 9606 (Homo sapiens)

VETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTD
PSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTK
AFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSA
GGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGY
PITLFVEK

Ligand information

• Ligand ID: MT0
• InChI: InChI=1S/C9H7ClN2/c1-6-7-4-2-3-5-8(7)9(10)12-11-6/h2-5H,1H3
• InChIKey: IEDBAGGSOLFBBH-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.352: Cc1nnc(Cl)c2ccccc12
  OpenEye OEToolkits 1.6.1: Cc1c2ccccc2c(nn1)Cl
  ACDLabs 10.04: Clc2nnc(c1c2cccc1)C
• Formula: C9 H7 Cl N2
• Name: 1-CHLORO-4-METHYLPHTHALAZINE
• ZINC: ZINC000000254692
• PDB chain: 2xdu Chain A Residue 1228

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2xdu Fragment-Based Drug Discovery Applied to Hsp90. Discovery of Two Lead Series with High Ligand Efficiency.
• Resolution: 1.74 Å
• Binding residue (original residue number in PDB): M98 L107 F138 Y139 W162
• Binding residue (residue number reindexed from 1): M82 L91 F122 Y123 W146
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 3.6.4.10: non-chaperonin molecular chaperone ATPase.

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

External links

• PDB: RCSB:2xdu, PDBe:2xdu, PDBj:2xdu
• PDBsum: 2xdu
• PubMed: 20718493
• UniProt: P07900|HS90A_HUMAN Heat shock protein HSP 90-alpha (Gene Name=HSP90AA1)