› 2zsg

X-ray diffraction
1.65Å resolution

Crystal structure of X-Pro aminopeptidase from Thermotoga maritima MSB8

Released:
DOI: 10.2210/pdb2zsg/pdb
PDB entry 2zsg coloured by chain, front view.
PDB entry 2zsg coloured by chain, side view.
PDB entry 2zsg coloured by chain, top view.
Source organism: Thermotoga maritima
Entry authors: Mizutani H, Kunishima N

Function and Biology Details

Reaction catalysed: 
Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminopeptidase P, putative Chains: A, B
Molecule details ›
Chains: A, B
Length: 359 amino acids
Theoretical weight: 39.99 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WXP9 (Residues: 1-359; Coverage: 100%)
Gene name: TM_0042
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand ZN 1 x ZN
Ligand NA 3 x NA
Ligand CL 4 x CL
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: C2
Unit cell:
a: 116.972Å b: 77.923Å c: 77.553Å
α: 90° β: 92.44° γ: 90°
R-values:
R R work R free
0.192 0.191 0.215
Expression system: Escherichia coli

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