› 4jn5

X-ray diffraction
2.44Å resolution

Crystal structures of the first condensation domain of the CDA synthetase

Released:
DOI: 10.2210/pdb4jn5/pdb
PDB entry 4jn5 coloured by chain, front view.
PDB entry 4jn5 coloured by chain, side view.
PDB entry 4jn5 coloured by chain, top view.
Source organism: Streptomyces coelicolor A3(2)
Primary publication:
Crystal structures of the first condensation domain of CDA synthetase suggest conformational changes during the synthetic cycle of nonribosomal peptide synthetases.
Bloudoff K, Rodionov D, Schmeing TM
J Mol Biol 425 3137-50 (2013)
PMID: 23756159

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195581 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carrier domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 450 amino acids
Theoretical weight: 48.53 KDa
Source organism: Streptomyces coelicolor A3(2)
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Z4X6 (Residues: 1-449; Coverage: 6%)
Gene names: SCE63.03c, SCO3230, cdaPSI
Sequence domains: Condensation domain
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P21
Unit cell:
a: 62.13Å b: 82.438Å c: 87.732Å
α: 90° β: 106.34° γ: 90°
R-values:
R R work R free
0.204 0.2 0.257
Expression system: Escherichia coli

Quick links

Citations

18 review citations

Nonribosomal Peptide Synthesis-Principles and Prospects.
Süssmuth et al. (2017)
17 more

5 mentions without citation

Structural advances toward understanding the catalytic activity and conformational dynamics of modular nonribosomal peptide synthetases.
Patel et al. (2023)
4 more