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Solution structure of apo groel by cryo-electron microscopy

Analyse Solution structure of apo groel by cryo-electron microscopy in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1GR5
Type
protein
Length
7,238 residues
Chains
14
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
60 kda chaperonin
UniProt
P0A6F6
Pockets
20 · best druggability 0.81

Structure

electron microscopy · 1 distinct chain · 51% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N60 kda chaperoninprotein51751% helix, 16% strandP0A6F6

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19640.810.83100empty
27990.800.8487empty
38880.800.8385empty
49540.800.8293empty
57540.790.8378empty

Interfaces

28 interfaces between chains.

  • H–I · 1990 Ų buried · 35 hydrogen bonds · protein-protein
  • H–N · 1988 Ų buried · 35 hydrogen bonds · protein-protein
  • I–J · 1988 Ų buried · 35 hydrogen bonds · protein-protein
  • M–N · 1987 Ų buried · 35 hydrogen bonds · protein-protein
  • J–K · 1985 Ų buried · 35 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 7 isopeptide (isopeptide).

Compared structures

  • 1GR5 · Solution Structure of apo GroEL by Cryo-Electron microscopy · the same entry in another collection · chain K against K, TM-score 1.00

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