› 7dkc

X-ray diffraction
1.86Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-110129 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dipeptidyl-peptidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 720 amino acids
Theoretical weight: 78.06 KDa
Source organism: Stenotrophomonas maltophilia R551-3
Expression system: Escherichia coli
UniProt:
  • Canonical: B4SLK2 (Residues: 1-720; Coverage: 100%)
Gene name: Smal_0807
Sequence domains: Peptidase S46

Ligands and Environments

2 bound ligands:
Ligand TYR 4 x TYR
Ligand GOL 6 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P21
Unit cell:
a: 67.85Å b: 74.32Å c: 153.32Å
α: 90° β: 94.15° γ: 90°
R-values:
R R work R free
0.173 0.171 0.21
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

7-Aminocoumarin-4-acetic Acid as a Fluorescent Probe for Detecting Bacterial Dipeptidyl Peptidase Activities in Water-in-Oil Droplets and in Bulk.
Nakamura et al. (2022)

1 mention without citation

Structural basis for an exceptionally strong preference for asparagine residue at the S2 subsite of Stenotrophomonas maltophilia dipeptidyl peptidase 7.
Nakamura et al. (2021)