› 5kil

X-ray diffraction
2.72Å resolution

Function and Biology Details

Reaction catalysed: 
4-amino-L-phenylalanyl-[CmlP-peptidyl-carrier-protein] + reduced acceptor + O(2) = 2-(4-aminophenyl)-L-seryl-[CmlP-peptidyl-carrier-protein] + acceptor + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123399 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-amino-L-phenylalanyl-[CmlP-peptidyl-carrier-protein] 3-hydroxylase Chain: A
Molecule details ›
Chain: A
Length: 551 amino acids
Theoretical weight: 62.26 KDa
Source organism: Streptomyces venezuelae ATCC 10712
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: F2RB80 (Residues: 1-532; Coverage: 100%)
Gene names: SVEN_0921, cmlA
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand FEO 1 x FEO
Ligand K 1 x K
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P43212
Unit cell:
a: 153.954Å b: 153.954Å c: 92.548Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.202 0.262
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Dioxygen Activation by Nonheme Diiron Enzymes: Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes.
Jasniewski et al. (2018)
6 other articles

2 mentions without citation

Diiron monooxygenases in natural product biosynthesis.
Komor et al. (2018)
1 more