› 1itq

X-ray diffraction
2.3Å resolution

HUMAN RENAL DIPEPTIDASE

Released:
DOI: 10.2210/pdb1itq/pdb
PDB entry 1itq coloured by chain, front view.
PDB entry 1itq coloured by chain, side view.
PDB entry 1itq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis.
Nitanai Y, Satow Y, Adachi H, Tsujimoto M
J Mol Biol 321 177-84 (2002)
PMID: 12144777

Function and Biology Details

Reactions catalysed: 
Hydrolysis of dipeptides.
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147727 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dipeptidase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 369 amino acids
Theoretical weight: 41.11 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P16444 (Residues: 17-385; Coverage: 93%)
Gene names: DPEP1, MDP, RDP
Sequence domains: Membrane dipeptidase (Peptidase family M19)
Structure domains: Metal-dependent hydrolases

Ligands and Environments

2 bound ligands:
Ligand NAG 4 x NAG
Ligand ZN 4 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 81.948Å b: 81.213Å c: 57.164Å
α: 90° β: 96.73° γ: 90°
R-values:
R R work R free
0.187 0.181 0.258
Expression system: Komagataella pastoris

Quick links

Citations

4 review citations

Inborn errors in the metabolism of glutathione.
Ristoff et al. (2007)
3 more

4 mentions without citation

Effects of Glycosylation on the Enzymatic Activity and Mechanisms of Proteases.
Goettig P. (2016)
3 more