› 3nyq

X-ray diffraction
1.43Å resolution

Malonyl-CoA Ligase Ternary Product Complex with Methylmalonyl-CoA and AMP bound

Released:
DOI: 10.2210/pdb3nyq/pdb
PDB entry 3nyq coloured by chain, front view.
PDB entry 3nyq coloured by chain, side view.
PDB entry 3nyq coloured by chain, top view.
Source organism: Streptomyces coelicolor
Primary publication:
Enzymatic extender unit generation for in vitro polyketide synthase reactions: structural and functional showcasing of Streptomyces coelicolor MatB.
Hughes AJ, Keatinge-Clay A
Chem Biol 18 165-76 (2011)
PMID: 21338915

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-192187 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fatty acid synthase Chain: A
Molecule details ›
Chain: A
Length: 505 amino acids
Theoretical weight: 52.79 KDa
Source organism: Streptomyces coelicolor
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9L0A2 (Residues: 1-485; Coverage: 100%)
Gene names: SCC24.15, SCO2444
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand MCA 1 x MCA
Ligand AMP 1 x AMP
Ligand CL 2 x CL
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: C2221
Unit cell:
a: 73.376Å b: 86.786Å c: 153.391Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.195 0.216
Expression system: Escherichia coli

Quick links

Citations

11 review citations

The structures of type I polyketide synthases.
Keatinge-Clay AT. (2012)
10 more

5 mentions without citation

Antimicrobial peptide resistance of Vibrio cholerae results from an LPS modification pathway related to nonribosomal peptide synthetases.
Henderson et al. (2014)
4 more