X-ray diffraction
1.6Å resolution

Crystal structure of an engineered TycA variant in complex with an O-propargyl-beta-Tyr-AMP analog

Source organism: Brevibacillus parabrevis
Primary publication:
Nonribosomal biosynthesis of backbone-modified peptides.
Nat Chem 10 282-287 (2018)
PMID: 29461527

Function and Biology Details

Reaction catalysed:
ATP + L-phenylalanine + H(2)O = AMP + diphosphate + D-phenylalanine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Tyrocidine synthase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 427 amino acids
Theoretical weight: 47.69 KDa
Source organism: Brevibacillus parabrevis
Expression system: Escherichia coli
  • Canonical: P09095 (Residues: 3-418; Coverage: 38%)
Gene name: tycA
Sequence domains: AMP-binding enzyme
Structure domains: N-terminal domain of ligase-like

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 59.574Å b: 60.245Å c: 247.804Å
α: 90° β: 90° γ: 90°
R R work R free
0.176 0.176 0.201
Expression system: Escherichia coli