› 1fno

X-ray diffraction
2.4Å resolution

PEPTIDASE T (TRIPEPTIDASE)

Released:
DOI: 10.2210/pdb1fno/pdb
PDB entry 1fno coloured by chain, front view.
PDB entry 1fno coloured by chain, side view.
PDB entry 1fno coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Primary publication:
Structure of peptidase T from Salmonella typhimurium.
Håkansson K, Miller CG
Eur J Biochem 269 443-50 (2002)
PMID: 11856302

Function and Biology Details

Reaction catalysed: 
Release of the N-terminal residue from a tripeptide.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150690 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidase T Chain: A
Molecule details ›
Chain: A
Length: 417 amino acids
Theoretical weight: 46.68 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli
UniProt:
  • Canonical: P26311 (Residues: 1-409; Coverage: 100%)
Gene names: STM1227, pepT
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 2 x ZN
Ligand SO4 2 x SO4
1 modified residue:
Ligand MSE 15 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: C2
Unit cell:
a: 132.374Å b: 46.036Å c: 96.591Å
α: 90° β: 116.11° γ: 90°
R-values:
R R work R free
0.222 0.222 0.261
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Carnosinases, their substrates and diseases.
Bellia et al. (2014)
1 more

6 mentions without citation

X-ray structure of ILL2, an auxin-conjugate amidohydrolase from Arabidopsis thaliana.
Bitto et al. (2009)
5 more