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Crystal structure of trans editing enzyme prox from E.COLI

Analyse Crystal structure of trans editing enzyme prox from E.COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2DXA
Type
protein
Length
158 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein ybak
UniProt
P0AAR3
Ligands
CL
Pockets
1 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein ybakprotein15827% helix, 32% strandP0AAR3

Ligands and binding sites

  • CL · Chloride ion · ion · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11660.630.8525empty

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

  • 2DXA · Crystal structure of trans editing enzyme ProX from E.coli · the same entry in another collection · chain A against A, TM-score 1.00
  • P0AAR3 · AlphaFold monomer V2.0 prediction for cys-TRNA(PRO)/CYS-TRNA(CYS) deacylase ybak (P0AAR3) · a predicted model of the same protein · chain A against A, TM-score 0.98

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