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Crystal structure of the HSPBP1 core domain

Analyse Crystal structure of the HSPBP1 core domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1XQR
Type
protein
Length
536 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
HSPBP1 protein
UniProt
Q9NZL4
Pockets
3 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 79% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BHSPBP1 proteinprotein26879% helix, 0% strandQ9NZL4

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13130.650.8143empty
23050.650.8137empty
33750.640.7839empty

Interfaces

1 interface between chains.

  • A–B · 834 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 modified (engineered).

Compared structures

  • 1XQR · Crystal structure of the HspBP1 core domain · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9NZL4 · AlphaFold monomer V2.0 prediction for HSP70-binding protein 1 (Q9NZL4) · a predicted model of the same protein · chain A against A, TM-score 0.98

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