X-ray diffraction
2.8Å resolution

Crystal structure of Aminipeptidase (M18 family) from Thermotoga Maritima

Source organism: Thermotoga maritima
Entry authors: Min T, Shapiro L, Burley SK, New York SGX Research Center for Structural Genomics (NYSGXRC)

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
Probable M18 family aminopeptidase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 450 amino acids
Theoretical weight: 50.93 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
  • Canonical: Q9WYJ9 (Residues: 2-451; Coverage: 100%)
Gene names: TM_0365, apeA
Sequence domains: Aminopeptidase I zinc metalloprotease (M18)
Structure domains:

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P213
Unit cell:
a: 191.225Å b: 191.225Å c: 191.225Å
α: 90° β: 90° γ: 90°
R R work R free
0.168 0.168 0.239
Expression system: Escherichia coli