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Methanococcus maripaludis chaperonin, closed conformation 3

Analyse Methanococcus maripaludis chaperonin, closed conformation 3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7R9U
Type
protein
Length
505 residues
Chains
1
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Chaperonin
UniProt
Q877G8
Pockets
6 · best druggability 0.83

Structure

electron microscopy · 1 distinct chain · 44% helix, 9% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
JChaperoninprotein50544% helix, 9% strandQ877G8

Pockets

6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19340.830.8497empty
23050.740.8647empty
31230.730.9336empty
41190.600.8520empty
5870.370.7619empty

Compared structures

  • 7R9U · Methanococcus maripaludis chaperonin, closed conformation 3 · the same entry in another collection · chain J against J, TM-score 1.00

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