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The crystal structure of phenylalanyl-tRNA synthetase from thermus thermophilus complexed with cognate trnaphe

Analyse The crystal structure of phenylalanyl-tRNA synthetase from thermus thermophilus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1EIY
Type
protein + RNA
Length
1,206 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
TRNA(PHE); Phenylalanyl-tRNA synthetase
EC
6.1.1.20
UniProt
Q5SGX1, P27001, Q5SGX2
Pockets
19 · best druggability 0.76

Structure

x-ray diffraction · 3 distinct chains · 31% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
CTRNA(PHE)rna76—Q5SGX1
APhenylalanyl-tRNA synthetase (EC 6.1.1.20)protein34539% helix, 19% strandP27001
BPhenylalanyl-tRNA synthetase (EC 6.1.1.20)protein78527% helix, 24% strandQ5SGX2

Pockets

19 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19880.760.7978empty
2610.690.9720empty
37330.670.7630empty
44660.660.7938empty
56720.660.7661empty

Interfaces

3 interfaces between chains.

  • A–B · 4317 Ų buried · 66 hydrogen bonds · protein-protein
  • C–B · 561 Ų buried · 8 hydrogen bonds · protein-nucleic
  • C–A · 347 Ų buried · 5 hydrogen bonds · protein-nucleic

Compared structures

  • 1EIY · The crystal structure of phenylalanyl-tRNA synthetase from thermus thermophilus complexed… · the same entry in another collection · chain C against C, TM-score 1.00
  • P27001 · AlphaFold monomer V2.0 prediction for phenylalanine--tRNA ligase alpha subunit (P27001) · a predicted model of the same protein · chain A against A, TM-score 0.77
  • Q5SGX2 · AlphaFold monomer V2.0 prediction for phenylalanine--tRNA ligase alpha subunit (Q5SGX2) · a predicted model of the same protein · chain B against A, TM-score 0.22

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