PDBe 5i1v

X-ray diffraction
1.84Å resolution

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

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

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
CrmK 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)
  • Canonical: H8Y6P5 (Residues: 1-500; Coverage: 100%)
Sequence domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P1
Unit cell:
a: 63.63Å b: 95.73Å c: 98.44Å
α: 95.18° β: 96.98° γ: 104.39°
R R work R free
0.162 0.161 0.194
Expression system: Escherichia coli BL21(DE3)