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Crystal structure of F2YRS

Analyse Crystal structure of F2YRS in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4HJR
Type
protein
Length
615 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tyrosine-tRNA ligase
EC
6.1.1.1
UniProt
Q57834
Pockets
3 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 50% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATyrosine-tRNA ligase (EC 6.1.1.1)protein30949% helix, 14% strandQ57834
BTyrosine-tRNA ligase (EC 6.1.1.1)protein30650% helix, 14% strandQ57834

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13890.760.8651empty
24040.760.8550empty
31170.410.7521empty

Interfaces

1 interface between chains.

  • A–B · 1415 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 4HJR · Crystal structure of F2YRS · 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 B against A, TM-score 0.99

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