› 6bpr

X-ray diffraction
1.96Å resolution

Crystal structure of cysteine, nitric oxide-bound ferrous form of the uncrosslinked F2-Tyr157 human cysteine dioxygenase

Released:
DOI: 10.2210/pdb6bpr/pdb
PDB entry 6bpr coloured by chain, front view.
PDB entry 6bpr coloured by chain, side view.
PDB entry 6bpr coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Probing the Cys-Tyr Cofactor Biogenesis in Cysteine Dioxygenase by the Genetic Incorporation of Fluorotyrosine.
Li J, Koto T, Davis I, Liu A
Biochemistry 58 2218-2227 (2019)
PMID: 30946568

Function and Biology Details

Reaction catalysed: 
L-cysteine + O(2) = 3-sulfinoalanine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172611 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cysteine dioxygenase type 1 Chain: A
Molecule details ›
Chain: A
Length: 200 amino acids
Theoretical weight: 22.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q16878 (Residues: 2-200; Coverage: 100%)
Gene name: CDO1
Sequence domains: Cysteine dioxygenase type I
Structure domains: Jelly Rolls

Ligands and Environments

5 bound ligands:
Ligand FE 1 x FE
Ligand CYS 1 x CYS
Ligand NO 1 x NO
Ligand SO4 3 x SO4
Ligand GOL 7 x GOL
1 modified residue:
Ligand F2Y 1 x F2Y

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P65
Unit cell:
a: 131.306Å b: 131.306Å c: 34.175Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.163 0.16 0.188
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Carbon-fluorine bond cleavage mediated by metalloenzymes.
Wang et al. (2020)
1 more

2 mentions without citation

Chemical modifications of proteins and their applications in metalloenzyme studies.
Naowarojna et al. (2021)
1 more