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Crystal structure of grpe from thermus thermophilus HB8

Analyse Crystal structure of grpe from thermus thermophilus HB8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3A6M
Type
protein
Length
332 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein grpe
UniProt
Q56236
Pockets
1 · best druggability 0.32

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein grpeprotein16846% helix, 19% strandQ56236
BProtein grpeprotein16446% helix, 21% strandQ56236

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1850.320.7420empty

Interfaces

1 interface between chains.

  • A–B · 3143 Ų buried · 23 hydrogen bonds · protein-protein

Compared structures

  • 3A6M · Crystal structure of GrpE from Thermus thermophilus HB8 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q56236 · AlphaFold monomer V2.0 prediction for protein grpe (Q56236) · a predicted model of the same protein · chain A against A, TM-score 0.92

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