› 1n2t

X-ray diffraction
2Å resolution

C-DES Mutant K223A with GLY Covalenty Linked to the PLP-cofactor

Released:
DOI: 10.2210/pdb1n2t/pdb
PDB entry 1n2t coloured by chain, front view.
PDB entry 1n2t coloured by chain, side view.
PDB entry 1n2t coloured by chain, top view.
Source organism: Synechocystis sp. PCC 6714
Primary publication:
Snapshots of the cystine lyase C-DES during catalysis. Studies in solution and in the crystalline state.
Kaiser JT, Bruno S, Clausen T, Huber R, Schiaretti F, Mozzarelli A, Kessler D
J Biol Chem 278 357-65 (2003)
PMID: 12386155

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: 386 amino acids
Theoretical weight: 42.38 KDa
Source organism: Synechocystis sp. PCC 6714
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9ZHG9 (Residues: 9-393; Coverage: 98%)
Gene name: c-des
Sequence domains: Aminotransferase class-V
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P212121
Unit cell:
a: 62.752Å b: 66.237Å c: 172.792Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.201 0.245
Expression system: Escherichia coli

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Citations

5 review citations

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