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Crystal structure of the allosteric-defective chaperonin groel E434K mutant

Analyse Crystal structure of the allosteric-defective chaperonin groel E434K mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2YEY
Type
protein
Length
7,336 residues
Chains
14
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
60 kda chaperonin
UniProt
P0A6F5
Pockets
20 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N60 kda chaperoninprotein52451% helix, 19% strandP0A6F5

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19910.790.81112empty
210820.790.8098empty
310080.790.80109empty
49940.780.80108empty
510550.780.80108empty

Interfaces

28 interfaces between chains.

  • K–L · 1923 Ų buried · 28 hydrogen bonds · protein-protein
  • D–E · 1826 Ų buried · 19 hydrogen bonds · protein-protein
  • F–G · 1808 Ų buried · 24 hydrogen bonds · protein-protein
  • M–N · 1801 Ų buried · 19 hydrogen bonds · protein-protein
  • A–G · 1791 Ų buried · 22 hydrogen bonds · protein-protein

Compared structures

  • 2YEY · Crystal structure of the allosteric-defective chaperonin GroEL E434K mutant · the same entry in another collection · chain K against K, TM-score 1.00

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