› 1elq

X-ray diffraction
1.8Å resolution

CRYSTAL STRUCTURE OF THE CYSTINE C-S LYASE C-DES

Released:
DOI: 10.2210/pdb1elq/pdb
PDB entry 1elq coloured by chain, front view.
PDB entry 1elq coloured by chain, side view.
PDB entry 1elq coloured by chain, top view.
Source organism: Synechocystis sp. PCC 6714
Primary publication:
Crystal structure of the cystine C-S lyase from Synechocystis: stabilization of cysteine persulfide for FeS cluster biosynthesis.
Clausen T, Kaiser JT, Steegborn C, Huber R, Kessler D
Proc Natl Acad Sci U S A 97 3856-61 (2000)
PMID: 10760256

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195654 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminotransferase class V domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 390 amino acids
Theoretical weight: 42.85 KDa
Source organism: Synechocystis sp. PCC 6714
Expression system: Bacteria
UniProt:
  • Canonical: Q9ZHG9 (Residues: 12-393; Coverage: 97%)
Gene name: c-des
Sequence domains: Aminotransferase class-V
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand K 2 x K
Ligand PLP 2 x PLP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P212121
Unit cell:
a: 62.4Å b: 65.4Å c: 170.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.198 0.249
Expression system: Bacteria

Quick links

Citations

10 review citations

Structure, function, and formation of biological iron-sulfur clusters.
Johnson et al. (2005)
9 more

3 mentions without citation

Natural history of S-adenosylmethionine-binding proteins.
Kozbial et al. (2005)
2 more