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Phenylalanyl tRNA synthetase complexed with phenylalanine

Analyse Phenylalanyl tRNA synthetase complexed with phenylalanine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1B70
Type
protein
Length
1,040 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phenylalanyl-tRNA synthetase
EC
6.1.1.20
UniProt
P27001, P27002
Ligands
PHE, MG
Pockets
17 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 28% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhenylalanyl-tRNA synthetase (EC 6.1.1.20)protein26531% helix, 28% strandP27001
BPhenylalanyl-tRNA synthetase (EC 6.1.1.20)protein77528% helix, 26% strandP27002

Ligands and binding sites

  • PHE · Phenylalanine · ligand · chains A
  • MG · Magnesium ion · metal · chains A, B

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

Pockets

17 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1790.740.9816empty
26360.690.7857PHE
32760.630.8130empty
43930.620.7735empty
53370.590.7743empty

Interfaces

1 interface between chains.

  • A–B · 4314 Ų buried · 77 hydrogen bonds · protein-protein

Compared structures

  • 1B70 · Phenylalanyl tRNA synthetase complexed with phenylalanine · the same entry in another collection · chain A against A, 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 0.97
  • P27002 · AlphaFold monomer V2.0 prediction for phenylalanine--tRNA ligase beta subunit (P27002) · a predicted model of the same protein · chain B against A, TM-score 0.97

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