4ruh

X-ray diffraction
2.25Å resolution

Crystal structure of Human Carnosinase-2 (CN2) in complex with inhibitor, Bestatin at 2.25 A

Released:
Source organism: Homo sapiens
Entry authors: pandya V, Kaushik A, Singh AK, Singh RP, Kumaran S

Function and Biology Details

Reaction catalysed:
Hydrolysis of dipeptides, preferentially hydrophobic dipeptides including prolyl amino acids.
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-188600 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytosolic non-specific dipeptidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 475 amino acids
Theoretical weight: 52.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96KP4 (Residues: 1-475; Coverage: 100%)
Gene names: CN2, CNDP2, CPGL, HEL-S-13, PEPA
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P212121
Unit cell:
a: 87.09Å b: 100.07Å c: 105.83Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.219 0.282
Expression system: Escherichia coli