4njr

X-ray diffraction
2.3Å resolution

Structural and kinetic bases for the metal preference of the M18 aminopeptidase from Pseudomonas aeruginosa

Released:

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable M18 family aminopeptidase 2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 429 amino acids
Theoretical weight: 46.71 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9HYZ3 (Residues: 1-429; Coverage: 100%)
Gene names: PA3247, apeB
Sequence domains: Aminopeptidase I zinc metalloprotease (M18)
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 4A
Spacegroup: R3
Unit cell:
a: 134.187Å b: 134.187Å c: 328.756Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.149 0.146 0.196
Expression system: Escherichia coli