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Arabidopsis OM64 TPR domain

Analyse Arabidopsis OM64 TPR domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6HPG
Type
protein
Length
755 residues
Chains
12
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2
Source
Arabidopsis thaliana
Molecule
Outer envelope protein 64, mitochondrial; Heat shock protein 90-4
UniProt
F4KCL7, O03986
Pockets
7 · best druggability 0.49

Structure

x-ray diffraction · resolution 2 · 4 distinct chains · 75% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, DOuter envelope protein 64, mitochondrialprotein12179% helix, 0% strandF4KCL7
B, C, E, FOuter envelope protein 64, mitochondrialprotein11781% helix, 0% strandF4KCL7
a, b, dHeat shock protein 90-4protein80% helix, 0% strandO03986
c, e, fHeat shock protein 90-4protein70% helix, 0% strandO03986

Pockets

7 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12860.490.7335empty
21010.450.7916empty
31830.440.7428empty
41260.390.7416empty
5960.380.7515empty

Interfaces

14 interfaces between chains.

  • A–a · 533 Ų buried · 16 hydrogen bonds · protein-protein
  • D–d · 532 Ų buried · 15 hydrogen bonds · protein-protein
  • C–c · 525 Ų buried · 13 hydrogen bonds · protein-protein
  • F–f · 522 Ų buried · 14 hydrogen bonds · protein-protein
  • B–b · 517 Ų buried · 13 hydrogen bonds · protein-protein

Compared structures

  • 6HPG · Arabidopsis OM64 tpr domain · the same entry in another collection · chain f against f, TM-score 1.00

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