› 2ecf

X-ray diffraction
2.8Å resolution

Crystal Structure of Dipeptidyl Aminopeptidase IV from Stenotrophomonas maltophilia

Released:
DOI: 10.2210/pdb2ecf/pdb
PDB entry 2ecf coloured by chain, front view.
PDB entry 2ecf coloured by chain, side view.
PDB entry 2ecf coloured by chain, top view.
Source organism: Stenotrophomonas maltophilia
Primary publication:
Dipeptidyl aminopeptidase IV from Stenotrophomonas maltophilia exhibits activity against a substrate containing a 4-hydroxyproline residue.
Nakajima Y, Ito K, Toshima T, Egawa T, Zheng H, Oyama H, Wu YF, Takahashi E, Kyono K, Yoshimoto T
J Bacteriol 190 7819-29 (2008)
PMID: 18820015

Function and Biology Details

Reaction catalysed: 
Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161179 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dipeptidyl peptidase IV Chain: A
Molecule details ›
Chain: A
Length: 741 amino acids
Theoretical weight: 82.18 KDa
Source organism: Stenotrophomonas maltophilia
Expression system: Escherichia coli
UniProt:
  • Canonical: P95782 (Residues: 1-741; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P43212
Unit cell:
a: 105.877Å b: 105.877Å c: 161.895Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.185 0.24
Expression system: Escherichia coli

Quick links

Citations

4 review citations

The versatility and adaptation of bacteria from the genus Stenotrophomonas.
Ryan et al. (2009)
3 more

6 mentions without citation

Structural insights into the Pseudomonas aeruginosa type VI virulence effector Tse1 bacteriolysis and self-protection mechanisms.
Ding et al. (2012)
5 more