› 7cxs

X-ray diffraction
1.83Å resolution

Crystal structure of CmnK, a L-Dap formation enzyme in capreomycin biosynthesis

Released:
DOI: 10.2210/pdb7cxs/pdb
PDB entry 7cxs coloured by chain, front view.
PDB entry 7cxs coloured by chain, side view.
PDB entry 7cxs coloured by chain, top view.
Source organism: Saccharothrix mutabilis subsp. capreolus
Primary publication:
Characterization of Enzymes Catalyzing the Formation of the Nonproteinogenic Amino Acid l-Dap in Capreomycin Biosynthesis.
Hsu SH, Zhang S, Huang SC, Wu TK, Xu Z, Chang CY
Biochemistry 60 77-84 (2021)
PMID: 33356147

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-108163 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ornithine cyclodeaminase Chains: A, B
Molecule details ›
Chains: A, B
Length: 352 amino acids
Theoretical weight: 37.21 KDa
Source organism: Saccharothrix mutabilis subsp. capreolus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A6YEI2 (Residues: 1-332; Coverage: 100%)
Gene name: cmnK
Sequence domains: Ornithine cyclodeaminase/mu-crystallin family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Unit cell:
a: 50.106Å b: 87.08Å c: 146.137Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.186 0.22
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 citation in other articles

Crystal structure of CmnB involved in the biosynthesis of the nonproteinogenic amino acid L-2,3-diaminopropionic acid.
Toh et al. (2023)
1 more