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Crystal structure of the TPR2A domain of hop in complex with the HSP90 peptide meevd

Analyse Crystal structure of the TPR2A domain of hop in complex with the HSP90 peptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1ELR
Type
protein
Length
133 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
TPR2A-domain of hop; HSP90-peptide meevd
UniProt
P31948
Ligands
ACE, NI
Pockets
1 · best druggability 0.48

Structure

x-ray diffraction · 2 distinct chains · 80% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATPR2A-domain of hopprotein12884% helix, 0% strandP31948
BHSP90-peptide meevdprotein50% helix, 0% strand—

Ligands and binding sites

  • ACE · Acetyl group · ligand · chains B
  • NI · Nickel (II) ion · metal · 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, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11570.480.7723empty

Interfaces

1 interface between chains.

  • A–B · 510 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

  • 1ELR · Crystal structure of the TPR2A domain of HOP in complex with the HSP90 peptide MEEVD · the same entry in another collection · chain A against A, TM-score 1.00
  • P31948 · AlphaFold monomer V2.0 prediction for stress-induced-phosphoprotein 1 (P31948) · a predicted model of the same protein · chain A against A, TM-score 0.98

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