› 5lp3

Electron Microscopy
10.5Å resolution

Three tetrameric rings of Isoaspartyl Dipeptidase fitted in an EM volume.

Released:
DOI: 10.2210/pdb5lp3/pdb
PDB entry 5lp3 coloured by chain, front view.
PDB entry 5lp3 coloured by chain, side view.
PDB entry 5lp3 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Proteins evolve on the edge of supramolecular self-assembly.
Garcia-Seisdedos H, Empereur-Mot C, Elad N, Levy ED
Nature 548 244-247 (2017)
PMID: 28783726
Related structures: EMD-4094

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153875 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isoaspartyl dipeptidase Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 390 amino acids
Theoretical weight: 41.17 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P39377 (Residues: 1-390; Coverage: 100%)
Gene names: JW4291, b4328, iadA, yjiF
Sequence domains: Amidohydrolase family

Ligands and Environments

No bound ligands
1 modified residue:
Ligand KCX 12 x KCX

Experiments and Validation Details

Entry percentile scores
Resolution: 10.5Å
Relevant EMDB volumes: EMD-4094
Expression system: Escherichia coli

Quick links

Citations

21 review citations

Multicomponent self-assembly as a tool to harness new properties from peptides and proteins in material design.
Okesola et al. (2018)
20 more