› 1pok

X-ray diffraction
2.7Å resolution

Crystal structure of Isoaspartyl Dipeptidase

Released:
DOI: 10.2210/pdb1pok/pdb
PDB entry 1pok coloured by chain, front view.
PDB entry 1pok coloured by chain, side view.
PDB entry 1pok coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
X-ray structure of isoaspartyl dipeptidase from E.coli: a dinuclear zinc peptidase evolved from amidohydrolases.
Jozic D, Kaiser JT, Huber R, Bode W, Maskos K
J Mol Biol 332 243-56 (2003)
PMID: 12946361

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo octamer
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-153874 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isoaspartyl dipeptidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 390 amino acids
Theoretical weight: 41.17 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P39377 (Residues: 1-390; Coverage: 100%)
Gene names: JW4291, b4328, iadA, yjiF
Sequence domains: Amidohydrolase family
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand SO4 2 x SO4
Ligand ZN 4 x ZN
Ligand ASN 2 x ASN
1 modified residue:
Ligand KCX 2 x KCX

Experiments and Validation Details

Entry percentile scores
Spacegroup: P4212
Unit cell:
a: 117.475Å b: 117.475Å c: 137.955Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.209 0.266

Quick links

Citations

1 review citation

Phosphinic Peptides as Tool Compounds for the Study of Pharmacologically Relevant Zn-Metalloproteases.
Georgiadis et al. (2022)
15 other articles

3 mentions without citation

Mutant libraries reveal negative design shielding proteins from supramolecular self-assembly and relocalization in cells.
Garcia Seisdedos et al. (2022)
2 more