› 2gdw

Solution NMR

Solution structure of the B. brevis TycC3-PCP in A/H-state

Released:
DOI: 10.2210/pdb2gdw/pdb
PDB entry 2gdw coloured by chain, ensemble of 19 models, front view.
PDB entry 2gdw coloured by chain, ensemble of 19 models, side view.
PDB entry 2gdw coloured by chain, ensemble of 19 models, top view.
Source organism: Brevibacillus parabrevis
Primary publication:
Conformational switches modulate protein interactions in peptide antibiotic synthetases.
Koglin A, Mofid MR, Löhr F, Schäfer B, Rogov VV, Blum MM, Mittag T, Marahiel MA, Bernhard F, Dötsch V
Science 312 273-6 (2006)
PMID: 16614225

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128244 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrocidine synthase 3 Chain: A
Molecule details ›
Chain: A
Length: 85 amino acids
Theoretical weight: 9.25 KDa
Source organism: Brevibacillus parabrevis
Expression system: Escherichia coli
UniProt:
  • Canonical: O30409 (Residues: 3032-3113; Coverage: 1%)
Gene name: tycC
Sequence domains: Phosphopantetheine attachment site
Structure domains: ACP-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: energy minimization
Expression system: Escherichia coli

Quick links

Citations

24 review citations

The role of dynamic conformational ensembles in biomolecular recognition.
Boehr et al. (2009)
23 more

6 mentions without citation

Structural insights into nonribosomal peptide enzymatic assembly lines.
Koglin et al. (2009)
5 more