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Crystal structure of tyrosine-tRNA synthetase from acinetobacter baumannii with bound L-tyrosine

Analyse Crystal structure of tyrosine-tRNA synthetase from acinetobacter baumannii with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6BQZ
Type
protein
Length
430 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
A0A086HYS2
Ligands
TYR, MG
Pockets
6 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 51% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATyrosine--tRNA ligase (EC 6.1.1.1)protein21552% helix, 14% strandA0A086HYS2
BTyrosine--tRNA ligase (EC 6.1.1.1)protein21550% helix, 14% strandA0A086HYS2

Ligands and binding sites

  • TYR · Tyrosine · ligand · 2 copies · chains A, B
  • MG · Magnesium ion · metal · 2 copies · chains A, B
  • ACT · Acetate ion · additive · chains B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13000.630.8037TYR
22830.620.8038TYR
3690.420.8017empty
4540.370.7916empty
5810.350.7619empty

Interfaces

1 interface between chains.

  • A–B · 469 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 6BQZ · Crystal Structure of Tyrosine-tRNA Synthetase from Acinetobacter baumannii with bound… · the same entry in another collection · chain A against A, TM-score 1.00

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