5i1w

X-ray diffraction
2.15Å resolution

Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis

Released:
Entry authors: Picard M-E, Barma J, Shi R

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-124896 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FAD-binding PCMH-type domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 500 amino acids
Theoretical weight: 55.29 KDa
Source organism: Actinoalloteichus sp. WH1-2216-6
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: H8Y6P5 (Residues: 1-500; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P1
Unit cell:
a: 63.11Å b: 95.2Å c: 98.04Å
α: 94.73° β: 96.56° γ: 105.2°
R-values:
R R work R free
0.171 0.168 0.213
Expression system: Escherichia coli BL21(DE3)