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Conformational variability in the refined structure of the chaperonin groel at 2.8 ångström resolution

Analyse Conformational variability in the refined structure of the chaperonin groel at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1OEL
Type
protein
Length
3,668 residues
Chains
7
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Groel (HSP60 class)
UniProt
P0A6F5
Pockets
20 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, GGroel (HSP60 class)protein52454% helix, 18% strandP0A6F5

Pockets

20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18720.790.8294empty
211270.780.8094empty
311470.780.8099empty
45240.730.8259empty
56400.730.8058empty

Interfaces

7 interfaces between chains.

  • B–C · 1698 Ų buried · 29 hydrogen bonds · protein-protein
  • E–F · 1659 Ų buried · 27 hydrogen bonds · protein-protein
  • A–B · 1651 Ų buried · 25 hydrogen bonds · protein-protein
  • F–G · 1650 Ų buried · 28 hydrogen bonds · protein-protein
  • D–E · 1642 Ų buried · 25 hydrogen bonds · protein-protein

Compared structures

  • 1OEL · Conformational variability in the refined structure of the chaperonin groel at 2.8… · the same entry in another collection · chain G against G, TM-score 1.00
  • P0A6F5 · AlphaFold monomer V2.0 prediction for 60 kda chaperonin (P0A6F5) · a predicted model of the same protein · chain C against A, TM-score 0.86

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