› 4q4e

X-ray diffraction
1.9Å resolution

Crystal structure of E.coli aminopeptidase N in complex with actinonin

Released:
DOI: 10.2210/pdb4q4e/pdb
PDB entry 4q4e coloured by chain, front view.
PDB entry 4q4e coloured by chain, side view.
PDB entry 4q4e coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural basis for the inhibition of M1 family aminopeptidases by the natural product actinonin: Crystal structure in complex with E. coli aminopeptidase N.
Ganji RJ, Reddi R, Gumpena R, Marapaka AK, Arya T, Sankoju P, Bhukya S, Addlagatta A
Protein Sci 24 823-31 (2015)
PMID: 25644575

Function and Biology Details

Reaction catalysed: 
Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138200 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminopeptidase N Chain: A
Molecule details ›
Chain: A
Length: 891 amino acids
Theoretical weight: 101.44 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P04825 (Residues: 1-870; Coverage: 100%)
Gene names: JW0915, b0932, pepN
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand ZN 1 x ZN
Ligand BB2 1 x BB2
Ligand GOL 8 x GOL
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P3121
Unit cell:
a: 120.45Å b: 120.45Å c: 170.748Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.149 0.147 0.181
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Small molecule inhibition of apicomplexan FtsH1 disrupts plastid biogenesis in human pathogens.
Amberg-Johnson et al. (2017)
3 more

3 mentions without citation

Marine Invertebrates: A Promissory Still Unexplored Source of Inhibitors of Biomedically Relevant Metallo Aminopeptidases Belonging to the M1 and M17 Families.
Pascual Alonso et al. (2023)
2 more