› 1f7t

X-ray diffraction
1.8Å resolution

Function and Biology Details

Reaction catalysed: 
CoA-(4'-phosphopantetheine) + an apo-[acyl-carrier-protein] = adenosine 3',5'-bisphosphate + an [acyl-carrier-protein]
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo trimer (preferred)
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-161229 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Holo-[acyl-carrier-protein] synthase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 122 amino acids
Theoretical weight: 13.69 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P96618 (Residues: 2-121; Coverage: 99%)
Gene names: BSU04620, acpS, ydcB
Sequence domains: 4'-phosphopantetheinyl transferase superfamily
Structure domains: 4'-phosphopantetheinyl transferase domain

Ligands and Environments

4 bound ligands:
Ligand NA 8 x NA
Ligand CL 19 x CL
Ligand DTT 5 x DTT
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21
Unit cell:
a: 76.262Å b: 76.16Å c: 85.693Å
α: 90° β: 93.32° γ: 90°
R-values:
R R work R free
0.197 0.196 0.219
Expression system: Escherichia coli

Quick links

Citations

22 review citations

Biosynthesis of nonribosomal peptides1.
Finking et al. (2004)
21 more

3 mentions without citation

The phosphopantetheinyl transferases: catalysis of a post-translational modification crucial for life.
Beld et al. (2014)
2 more