› 2aqv

X-ray diffraction
1.95Å resolution

Crystal Structure of E. coli Isoaspartyl Dipeptidase mutant Y137F

Released:
DOI: 10.2210/pdb2aqv/pdb
PDB entry 2aqv coloured by chain, front view.
PDB entry 2aqv coloured by chain, side view.
PDB entry 2aqv coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Functional significance of Glu-77 and Tyr-137 within the active site of isoaspartyl dipeptidase.
Martí-Arbona R, Thoden JB, Holden HM, Raushel FM
Bioorg Chem 33 448-58 (2005)
PMID: 16289685

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153878 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isoaspartyl dipeptidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 390 amino acids
Theoretical weight: 41.15 KDa
Source organism: Escherichia coli
Expression system: 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

1 bound ligand:
Ligand ZN 4 x ZN
1 modified residue:
Ligand KCX 2 x KCX

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P4212
Unit cell:
a: 119.1Å b: 119.1Å c: 138.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.183 0.213
Expression system: Escherichia coli

Quick links

Citations

5 citation in other articles

The crystal structures of dihydropyrimidinases reaffirm the close relationship between cyclic amidohydrolases and explain their substrate specificity.
Lohkamp et al. (2006)
4 more

2 mentions without citation

Do we see what we should see? Describing non-covalent interactions in protein structures including precision.
Gurusaran et al. (2014)
1 more