Function and Biology Details
Reactions catalysed:
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins
ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp)
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Aspartate--tRNA(Asp) ligase and Lysozyme C (preferred)
PDBe Complex ID:
PDB-CPX-523794 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Lysozyme C
Molecule details ›
Chains: A, B
Length: 129 amino acids
Theoretical weight: 14.33 KDa
Source organism: Gallus gallus
UniProt:
Sequence domains: C-type lysozyme/alpha-lactalbumin family
Structure domains: Lysozyme
Length: 129 amino acids
Theoretical weight: 14.33 KDa
Source organism: Gallus gallus
UniProt:
- Canonical:
P00698 (Residues: 19-147; Coverage: 100%)
Sequence domains: C-type lysozyme/alpha-lactalbumin family
Structure domains: Lysozyme
Aspartate--tRNA(Asp) ligase
Molecule details ›
Chains: C, D
Length: 109 amino acids
Theoretical weight: 11.76 KDa
Source organism: Pyrobaculum aerophilum
Expression system: Escherichia coli DH5[alpha]
UniProt:
Sequence domains: OB-fold nucleic acid binding domain
Structure domains: Nucleic acid-binding proteins
Length: 109 amino acids
Theoretical weight: 11.76 KDa
Source organism: Pyrobaculum aerophilum
Expression system: Escherichia coli DH5[alpha]
UniProt:
- Canonical: Q8ZYM8 (Residues: 1-46, 47-104; Coverage: 24%)
Sequence domains: OB-fold nucleic acid binding domain
Structure domains: Nucleic acid-binding proteins
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SSRL
Spacegroup:
P41212
Expression system: Escherichia coli DH5[alpha]
