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D7 symmetrized structure of unliganded groel at 4.2 ångström resolution by cryoem

Analyse D7 symmetrized structure of unliganded groel at 4.2 ångström resolution by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3CAU
Type
protein
Length
7,364 residues
Chains
14
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
60 kda chaperonin
UniProt
P0A6F5
Pockets
18 · best druggability 0.56

Structure

electron microscopy · 1 distinct chain · 0% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N60 kda chaperoninprotein5260% helix, 0% strandP0A6F5

Pockets

18 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13350.560.7357empty
23360.550.7365empty
32990.530.7360empty
43020.530.7360empty
52930.530.7355empty

Interfaces

19 interfaces between chains.

  • H–I · 197 Ų buried · 0 hydrogen bonds · protein-protein
  • F–G · 195 Ų buried · 0 hydrogen bonds · protein-protein
  • J–K · 195 Ų buried · 0 hydrogen bonds · protein-protein
  • M–N · 194 Ų buried · 0 hydrogen bonds · protein-protein
  • C–D · 193 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 3CAU · D7 symmetrized structure of unliganded GroEL at 4.2 Angstrom resolution by cryoEM · the same entry in another collection · chain K against K, TM-score 1.00

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