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MolNFT v1 · #8113 · protein

Solution structure of apo groel by cryo-electron microscopy

1GR5 · 60 kda chaperonin: “Solution structure of apo groel by cryo-electron microscopy”. Electron microscopy, 20 pockets (best druggability 0.81). MolNFT v1 #8113 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

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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