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Crystal structure of sefrs

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

PDB
7C5C
Type
protein
Length
312 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tyrosine--tRNA ligase
EC
6.1.1.1
UniProt
Q57834
Pockets
1 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATyrosine--tRNA ligase (EC 6.1.1.1)protein31251% helix, 13% strandQ57834

Ligands and binding sites

  • EDO · 1,2-ethanediol · additive · 2 copies · 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
13510.700.8342EDO

Compared structures

  • 7C5C · Crystal structure of SeFRS · the same entry in another collection · chain A against A, TM-score 1.00
  • Q57834 · AlphaFold monomer V2.0 prediction for tyrosine--tRNA ligase (Q57834) · a predicted model of the same protein · chain A against A, TM-score 0.96

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