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L89V, L93I and V136M mutant of N-term HSP90 complexed with geldanamycin

Analyse L89V, L93I and V136M mutant of N-term HSP90 complexed with geldanamycin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2YGF
Type
protein
Length
213 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ATP-dependent molecular chaperone HSP82
UniProt
P02829
Ligands
GDM
Pockets
1 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AATP-dependent molecular chaperone HSP82protein21343% helix, 23% strandP02829

Ligands and binding sites

  • GDM · Geldanamycin · ligand · chains A
  • GOL · Glycerol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12340.620.8126GDM

Compared structures

  • 2YGF · L89V, L93I and V136M Mutant of N-Term HSP90 complexed with Geldanamycin · the same entry in another collection · chain A against A, TM-score 1.00
  • P02829 · AlphaFold monomer V2.0 prediction for ATP-dependent molecular chaperone HSP82 (P02829) · a predicted model of the same protein · chain A against A, TM-score 0.82

Analyse

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