Brand  (β version)

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
GLY Glycine
K Potassium ion
PLP Pyridoxal-5'-phosphate
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 1N2T   PDBj   RCSB PDB   PDBe
Header : LYASE
Title : C-DES Mutant K223A with GLY Covalenty Linked to the PLP-cofactor
Release Data : 2003-01-21
Compound :
mol_id molecule chains
1 L-cysteine/cystine lyase C-DES A,B
ec: 4.4.1.-
mutation: K223A
Source :
mol_id organism_scientific expression_system
1 Synechocystis sp. PCC 6714  (taxid:1147) Escherichia coli  (taxid:562)
gene: C-DES
expression_system_vector_type: PLASMID
expression_system_plasmid: PSA15-PUC19
Authors : Kaiser, J.T., Bruno, S., Clausen, T., Huber, R., Schiaretti, F., Mozzarelli, A., Kessler, D.
Keywords : FES CLUSTER BIOSYNTHESIS, NIFS, PYRIDOXAL 5'-PHOSPHATE, INACTIVE MUTANT, LYASE
Exp. method : X-RAY DIFFRACTION ( 2.00 Å )
Citation :

Snapshots of the Cystine Lyase "C-DES" during Catalysis: Studies in Solution and in the Crystalline State

Kaiser, J.T.,Bruno, S.,Clausen, T.  et al.
(2003)  J.Biol.Chem.  278 : 357 - 365

PubMed: 12386155
DOI: 10.1074/jbc.M209862200