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Visualizing groel-es in the act of encapsulating a non-native substrate protein

Analyse Visualizing groel-es in the act of encapsulating a non-native substrate protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3ZQ0
Type
protein
Length
8,015 residues
Chains
21
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
60 kda chaperonin; 10 kda chaperonin
UniProt
P0A6F5, P0A6F9
Ligands
ADP, MG
Pockets
20 · best druggability 0.81

Structure

electron microscopy · 2 distinct chains · 44% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N60 kda chaperoninprotein52451% helix, 17% strandP0A6F5
O, P, Q, R, S, T, U10 kda chaperoninprotein973% helix, 37% strandP0A6F9

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · 7 copies · chains A, B, C, D, E, F, G
  • MG · Magnesium ion · metal · 7 copies · chains A, B, C, D, E, F, G

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17240.810.8593ADP, MG
27020.800.8484ADP, MG
33990.800.8969ADP, MG
46810.800.8489ADP, MG
53960.790.8960ADP, MG

Interfaces

49 interfaces between chains.

  • F–G · 1860 Ų buried · 20 hydrogen bonds · protein-protein
  • C–D · 1793 Ų buried · 22 hydrogen bonds · protein-protein
  • E–F · 1784 Ų buried · 23 hydrogen bonds · protein-protein
  • J–K · 1779 Ų buried · 25 hydrogen bonds · protein-protein
  • H–N · 1753 Ų buried · 22 hydrogen bonds · protein-protein

Compared structures

  • 3ZQ0 · Visualizing GroEL-ES in the Act of Encapsulating a Non-Native Substrate Protein · the same entry in another collection · chain I against I, TM-score 1.00

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