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Methanococcus maripaludis chaperonin, closed conformation 2

Analyse Methanococcus maripaludis chaperonin, closed conformation 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7R9M
Type
protein
Length
505 residues
Chains
1
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Chaperonin
UniProt
Q877G8
Pockets
11 · best druggability 0.82

Structure

electron microscopy · 1 distinct chain · 47% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
JChaperoninprotein50547% helix, 8% strandQ877G8

Pockets

11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16190.820.8770empty
21290.780.9532empty
32440.710.8638empty
4610.520.8723empty
51210.500.8016empty

Compared structures

  • 7R9M · Methanococcus maripaludis chaperonin, closed conformation 2 · the same entry in another collection · chain J against J, TM-score 1.00

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