› 4twe

X-ray diffraction
1.75Å resolution

Structure of ligand-free N-acetylated-alpha-linked-acidic-dipeptidase like protein (NAALADaseL)

Released:
DOI: 10.2210/pdb4twe/pdb
PDB entry 4twe coloured by chain, front view.
PDB entry 4twe coloured by chain, side view.
PDB entry 4twe coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and biochemical characterization of a novel aminopeptidase from human intestine.
Tykvart J, Bařinka C, Svoboda M, Navrátil V, Souček R, Hubálek M, Hradilek M, Šácha P, Lubkowski J, Konvalinka J
J Biol Chem 290 11321-36 (2015)
PMID: 25752612

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194073 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Aminopeptidase NAALADL1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 743 amino acids
Theoretical weight: 81.27 KDa
Source organism: Homo sapiens
Expression system: Drosophila melanogaster
UniProt:
  • Canonical: Q9UQQ1 (Residues: 28-740; Coverage: 96%)
Gene names: NAALADASEL, NAALADL, NAALADL1
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
5 bound ligands:
Ligand ZN 4 x ZN
Ligand CA 2 x CA
Ligand NAG 7 x NAG
Ligand GOL 7 x GOL
Ligand PEG 3 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: I222
Unit cell:
a: 98.512Å b: 174.844Å c: 208.034Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.167 0.188
Expression system: Drosophila melanogaster

Quick links

Citations

6 citation in other articles

Mouse glutamate carboxypeptidase II (GCPII) has a similar enzyme activity and inhibition profile but a different tissue distribution to human GCPII.
Knedlík et al. (2017)
5 more

5 mentions without citation

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