› 1mc1

X-ray diffraction
2.16Å resolution

BETA-LACTAM SYNTHETASE WITH PRODUCT (DGPC), AMP AND PPI

Released:
DOI: 10.2210/pdb1mc1/pdb
PDB entry 1mc1 coloured by chain, front view.
PDB entry 1mc1 coloured by chain, side view.
PDB entry 1mc1 coloured by chain, top view.
Source organism: Streptomyces clavuligerus
Primary publication:
The catalytic cycle of beta -lactam synthetase observed by x-ray crystallographic snapshots.
Miller MT, Bachmann BO, Townsend CA, Rosenzweig AC
Proc Natl Acad Sci U S A 99 14752-7 (2002)
PMID: 12409610

Function and Biology Details

Reaction catalysed: 
ATP + L-N(2)-(2-carboxyethyl)arginine = AMP + diphosphate + deoxyamidinoproclavaminate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143602 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carboxyethyl-arginine beta-lactam-synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 513 amino acids
Theoretical weight: 54.6 KDa
Source organism: Streptomyces clavuligerus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0DJQ7 (Residues: 1-513; Coverage: 100%)
Gene name: bls
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand MG 4 x MG
Ligand POP 2 x POP
Ligand AMP 2 x AMP
Ligand PCX 2 x PCX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P21
Unit cell:
a: 61.038Å b: 96.57Å c: 80.912Å
α: 90° β: 90.54° γ: 90°
R-values:
R R work R free
0.208 0.208 0.247
Expression system: Escherichia coli BL21(DE3)

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Citations

10 review citations

Asparagine synthetase chemotherapy.
Richards et al. (2006)
9 more

6 mentions without citation

Organization and evolution of the cotG and cotH genes of Bacillus subtilis.
Giglio et al. (2011)
5 more