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Crystal structure of tryptophanyl-tRNA synthetase from thermus thermophilus

Analyse Crystal structure of tryptophanyl-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
2EL7
Type
protein
Length
634 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tryptophanyl-tRNA synthetase
EC
6.1.1.2
UniProt
Q5SIY7
Ligands
PO4
Pockets
4 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 59% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATryptophanyl-tRNA synthetase (EC 6.1.1.2)protein31861% helix, 8% strandQ5SIY7
BTryptophanyl-tRNA synthetase (EC 6.1.1.2)protein31658% helix, 8% strandQ5SIY7

Ligands and binding sites

  • PO4 · Phosphate ion · ion · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17170.750.8065empty
26900.740.8057empty
31220.410.7627empty
4540.310.7716empty

Interfaces

1 interface between chains.

  • A–B · 2152 Ų buried · 19 hydrogen bonds · protein-protein

Compared structures

  • 2EL7 · Crystal structure of Tryptophanyl-tRNA synthetase from Thermus thermophilus · the same entry in another collection · chain A against A, TM-score 1.00

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