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Thermus thermophilus arginyl-tRNA synthetase

Analyse Thermus thermophilus arginyl-tRNA synthetase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1IQ0
Type
protein
Length
588 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Arginyl-tRNA synthetase
EC
6.1.1.19
UniProt
Q93RP5
Pockets
5 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AArginyl-tRNA synthetase (EC 6.1.1.19)protein58848% helix, 15% strandQ93RP5

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16700.720.7967empty
2520.340.7813empty
3500.310.7715empty
4790.310.7314empty
5510.260.7313empty

Compared structures

  • 1IQ0 · Thermus thermophilus arginyl-tRNA synthetase · the same entry in another collection · chain A against A, TM-score 1.00

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