5vl1

X-ray diffraction
2.7Å resolution

Crystal Structure of Lysyl-tRNA Synthetase from Mycobacterium ulcerans complexed with L-lysine

Released:
Source organism: Mycobacterium ulcerans Agy99
Entry author: Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

Reaction catalysed:
ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys)
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysine--tRNA ligase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 506 amino acids
Theoretical weight: 56.58 KDa
Source organism: Mycobacterium ulcerans Agy99
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0PV47 (Residues: 1-498; Coverage: 100%)
Gene names: MUL_4181, lysS
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P1
Unit cell:
a: 95.04Å b: 96.69Å c: 105.56Å
α: 90.38° β: 104.84° γ: 117.15°
R-values:
R R work R free
0.178 0.177 0.204
Expression system: Escherichia coli BL21(DE3)