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Peptide-binding domain of heat shock 70 kda protein F, mitochondrial precursor, from caenorhabditis elegans.

Analyse Peptide-binding domain of heat shock 70 kda protein F, mitochondrial precursor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3DQG
Type
protein
Length
581 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Heat shock 70 kda protein F
UniProt
P11141
Pockets
4 · best druggability 0.83

Structure

x-ray diffraction · 3 distinct chains · 13% helix, 46% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BHeat shock 70 kda protein Fprotein14814% helix, 45% strandP11141
CHeat shock 70 kda protein Fprotein13811% helix, 48% strandP11141
DHeat shock 70 kda protein Fprotein14714% helix, 45% strandP11141

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18740.830.8592empty
21240.550.8326empty
31670.540.8026empty
4750.310.7416empty

Interfaces

6 interfaces between chains.

  • C–D · 1776 Ų buried · 30 hydrogen bonds · protein-protein
  • A–B · 1716 Ų buried · 27 hydrogen bonds · protein-protein
  • B–D · 625 Ų buried · 14 hydrogen bonds · protein-protein
  • A–D · 203 Ų buried · 3 hydrogen bonds · protein-protein
  • A–C · 84 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 3DQG · Peptide-binding domain of heat shock 70 kDa protein F, mitochondrial precursor, from… · the same entry in another collection · chain A against A, TM-score 1.00
  • P11141 · AlphaFold monomer V2.0 prediction for heat shock protein HSP-6 (P11141) · a predicted model of the same protein · chain C against A, TM-score 0.78

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