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Crystal structures of a group II chaperonin from methanococcus maripaludis

Analyse Crystal structures of a group II chaperonin from methanococcus maripaludis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3KFK
Type
protein
Length
1,945 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Chaperonin
UniProt
Q877G8
Ligands
AGS
Pockets
20 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CChaperoninprotein48747% helix, 15% strandQ877G8
DChaperoninprotein48446% helix, 16% strandQ877G8

Ligands and binding sites

  • AGS · Phosphothiophosphoric acid-adenylate ester · ligand · 4 copies · chains A, B, C, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111620.790.80109AGS
210570.770.79109AGS
310380.770.7998AGS
47480.770.8186AGS
5500.690.9715empty

Interfaces

3 interfaces between chains.

  • C–D · 1006 Ų buried · 18 hydrogen bonds · protein-protein
  • A–B · 986 Ų buried · 21 hydrogen bonds · protein-protein
  • B–C · 974 Ų buried · 20 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 3KFK · Crystal structures of a group II chaperonin from Methanococcus maripaludis · the same entry in another collection · chain A against A, TM-score 1.00

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