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CryoEM structure of nucleotide-free GroEL-Rubisco.

Analyse CryoEM structure of nucleotide-free GroEL-Rubisco. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
8BA7
Type
protein
Length
7,336 residues
Chains
14
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
4.4
Source
Escherichia coli
Molecule
Chaperonin GroEL
EC
5.6.1.7
UniProt
P0A6F5
Pockets
20 · best druggability 0.78

Structure

electron microscopy · resolution 4.4 · 1 distinct chain · 53% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, NChaperonin GroEL (EC 5.6.1.7)protein52453% helix, 17% strandP0A6F5

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110200.780.80104empty
29080.780.8097empty
39970.770.79102empty
48590.770.8087empty
511050.760.79113empty

Interfaces

28 interfaces between chains.

  • H–N · 1588 Ų buried · 18 hydrogen bonds · protein-protein
  • E–F · 1586 Ų buried · 19 hydrogen bonds · protein-protein
  • L–M · 1577 Ų buried · 19 hydrogen bonds · protein-protein
  • M–N · 1572 Ų buried · 19 hydrogen bonds · protein-protein
  • D–E · 1566 Ų buried · 25 hydrogen bonds · protein-protein

Compared structures

  • P0A6F5 · AlphaFold monomer V2.0 prediction for 60 kda chaperonin (P0A6F5) · a predicted model of the same protein · chain A against A, TM-score 0.87

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