› 2wok

X-ray diffraction
1.7Å resolution

Clavulanic acid biosynthesis oligopeptide binding protein 2 complexed with bradykinin

Released:
DOI: 10.2210/pdb2wok/pdb
PDB entry 2wok coloured by chain, front view.
PDB entry 2wok coloured by chain, side view.
PDB entry 2wok coloured by chain, top view.
Source organisms:
Primary publication:
Crystal structures of an oligopeptide-binding protein from the biosynthetic pathway of the beta-lactamase inhibitor clavulanic acid.
Mackenzie AK, Valegård K, Iqbal A, Caines ME, Kershaw NJ, Jensen SE, Schofield CJ, Andersson I
J Mol Biol 396 332-44 (2010)
PMID: 19941870

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133906 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Solute-binding protein family 5 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 562 amino acids
Theoretical weight: 62.07 KDa
Source organism: Streptomyces clavuligerus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8KRB4 (Residues: 1-562; Coverage: 100%)
Gene names: SCLAV_4183, oppA2
Sequence domains: Bacterial extracellular solute-binding proteins, family 5 Middle
Structure domains:
Bradykinin Chain: B
Molecule details ›
Chain: B
Length: 9 amino acids
Theoretical weight: 1.06 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P01042 (Residues: 381-389; Coverage: 1%)
Gene names: BDK, KNG, KNG1

Ligands and Environments

1 bound ligand:
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P21
Unit cell:
a: 53.511Å b: 83.327Å c: 62.38Å
α: 90° β: 95.54° γ: 90°
R-values:
R R work R free
0.187 0.185 0.223
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

4 review citations

The enzymes of β-lactam biosynthesis.
Hamed et al. (2013)
3 more

2 mentions without citation

Unconventional N-H…N Hydrogen Bonds Involving Proline Backbone Nitrogen in Protein Structures.
Deepak et al. (2016)
1 more