› 2qtp

X-ray diffraction
2.1Å resolution

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-177573 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptide synthase Chain: A
Molecule details ›
Chain: A
Length: 194 amino acids
Theoretical weight: 20.81 KDa
Source organism: Ruegeria pomeroyi DSS-3
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5LV76 (Residues: 1-193; Coverage: 100%)
Gene name: SPO0826
Sequence domains: Amino acid synthesis
Structure domains: BB2672

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 5 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P43212
Unit cell:
a: 94.73Å b: 94.73Å c: 47.15Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.204 0.259
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Elucidation of the trigonelline degradation pathway reveals previously undescribed enzymes and metabolites.
Perchat et al. (2018)
1 more

2 mentions without citation

Decision-making in structure solution using Bayesian estimates of map quality: the PHENIX AutoSol wizard.
Terwilliger et al. (2009)
1 more