› 1y2g

X-ray diffraction
1.9Å resolution

Crystal STructure of ZipA in complex with an inhibitor

Released:
DOI: 10.2210/pdb1y2g/pdb
PDB entry 1y2g coloured by chain, front view.
PDB entry 1y2g coloured by chain, side view.
PDB entry 1y2g coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
A shape-based 3-D scaffold hopping method and its application to a bacterial protein-protein interaction.
Rush TS, Grant JA, Mosyak L, Nicholls A
J Med Chem 48 1489-95 (2005)
PMID: 15743191

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160123 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cell division protein ZipA Chains: A, B
Molecule details ›
Chains: A, B
Length: 140 amino acids
Theoretical weight: 15.66 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P77173 (Residues: 189-328; Coverage: 43%)
Gene names: JW2404, b2412, zipA
Sequence domains: ZipA, C-terminal FtsZ-binding domain
Structure domains: ZipA, C-terminal FtsZ-binding domain

Ligands and Environments

1 bound ligand:
Ligand CL3 1 x CL3
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 52.695Å b: 39.521Å c: 70.271Å
α: 90° β: 104.97° γ: 90°
R-values:
R R work R free
0.207 0.207 0.241
Expression system: Not provided

Quick links

Citations

46 review citations

Reaching for high-hanging fruit in drug discovery at protein-protein interfaces.
Wells et al. (2007)
45 more

4 mentions without citation

Modulating protein-protein interactions with small molecules: the importance of binding hotspots.
Thangudu et al. (2012)
3 more