› 3vat

X-ray diffraction
2.1Å resolution

Crystal structure of DNPEP, ZnMg form

Released:
DOI: 10.2210/pdb3vat/pdb
PDB entry 3vat coloured by chain, front view.
PDB entry 3vat coloured by chain, side view.
PDB entry 3vat coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Insights into substrate specificity and metal activation of mammalian tetrahedral aspartyl aminopeptidase.
Chen Y, Farquhar ER, Chance MR, Palczewski K, Kiser PD
J Biol Chem 287 13356-70 (2012)
PMID: 22356908

Function and Biology Details

Reaction catalysed: 
Release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173622 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartyl aminopeptidase Chain: A
Molecule details ›
Chain: A
Length: 496 amino acids
Theoretical weight: 55.04 KDa
Source organism: Bos taurus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q2HJH1 (Residues: 3-471; Coverage: 100%)
Gene name: DNPEP
Sequence domains: Aminopeptidase I zinc metalloprotease (M18)
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: F432
Unit cell:
a: 244.269Å b: 244.269Å c: 244.269Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.17 0.211
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

Flexibility and reactivity in promiscuous enzymes.
Gatti-Lafranconi et al. (2013)
17 other articles

5 mentions without citation

Insights into substrate specificity and metal activation of mammalian tetrahedral aspartyl aminopeptidase.
Chen et al. (2012)
4 more