› 3dlj

X-ray diffraction
2.26Å resolution

Crystal structure of human carnosine dipeptidase 1

Released:
DOI: 10.2210/pdb3dlj/pdb
PDB entry 3dlj coloured by chain, front view.
PDB entry 3dlj coloured by chain, side view.
PDB entry 3dlj coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Dong A, Dobrovetsky E, Seitova A, He H, Tempel W, Kozieradzki I, Arrowsmith CH, Weigelt J, Bountra C, Edwards AM, Bochkarev A, Cossar D, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed: 
Preferential hydrolysis of the beta-Ala-|-His dipeptide (carnosine), and also anserine, Xaa-|-His dipeptides and other dipeptides including homocarnosine.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-188598 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-Ala-His dipeptidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 485 amino acids
Theoretical weight: 54.3 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q96KN2 (Residues: 27-507; Coverage: 100%)
Gene names: CN1, CNDP1, CPGL2, UNQ1915/PRO4380
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand ZN 4 x ZN
Ligand UNX 15 x UNX
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P21
Unit cell:
a: 77.106Å b: 75.613Å c: 103.716Å
α: 90° β: 109.79° γ: 90°
R-values:
R R work R free
0.201 0.2 0.254
Expression system: Spodoptera frugiperda

Quick links