› 1j3g

Solution NMR

Solution structure of Citrobacter Freundii AmpD

Released:
DOI: 10.2210/pdb1j3g/pdb
PDB entry 1j3g coloured by chain, ensemble of 20 models, front view.
PDB entry 1j3g coloured by chain, ensemble of 20 models, side view.
PDB entry 1j3g coloured by chain, ensemble of 20 models, top view.
Source organism: Citrobacter freundii
Primary publication:
NMR structure of Citrobacter freundii AmpD, comparison with bacteriophage T7 lysozyme and homology with PGRP domains.
Liepinsh E, Généreux C, Dehareng D, Joris B, Otting G
J Mol Biol 327 833-42 (2003)
PMID: 12654266

Function and Biology Details

Reaction catalysed: 
Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160659 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD Chain: A
Molecule details ›
Chain: A
Length: 187 amino acids
Theoretical weight: 20.87 KDa
Source organism: Citrobacter freundii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P82974 (Residues: 1-187; Coverage: 100%)
Gene name: ampD
Sequence domains: N-acetylmuramoyl-L-alanine amidase
Structure domains: Peptidoglycan recognition protein-like

Ligands and Environments

1 bound ligand:
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli BL21(DE3)

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Citations

14 review citations

The immune response of Drosophila.
Hoffmann JA. (2003)
13 more

5 mentions without citation

Cell Wall Hydrolases in Bacteria: Insight on the Diversity of Cell Wall Amidases, Glycosidases and Peptidases Toward Peptidoglycan.
Vermassen et al. (2019)
4 more