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
F42 Coenzyme f420
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 3R5R   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : Structure of Ddn, the Deazaflavin-dependent nitroreductase from Mycobacterium tuberculosis involved in bioreductive activation of PA-824, with co-factor F420
Release Data : 2012-01-18
Compound :
mol_id molecule chains
1 Deazaflavin-dependent nitroreductase A,B,C,D,E
ec: 1.-.-.-
Source :
mol_id organism_scientific expression_system
1 Mycobacterium tuberculosis  (taxid:1773) Escherichia coli  (taxid:562)
gene: ddn, MT3651, Rv3547
expression_system_vector_type: plasmid
expression_system_plasmid: SpeedET
Authors : Cellitti, S.E., Shaffer, J., Jones, D.H., Mukherjee, T., Gurumurthy, M., Bursulaya, B., Boshoff, H.I.M., Choi, I., Nayya, A., Lee, Y.S., Cherian, J., Niyomrattanakit, P., Dick, T., Manjunatha, U.H., Barry, C.E., Spraggon, G., Geierstanger, B.H.
Keywords : PA-824, split barrel-like fold, DUF385, Deazaflavin-dependent nitroreductase, co-factor, nitroimidazoles, OXIDOREDUCTASE
Exp. method : X-RAY DIFFRACTION ( 2.1010 Å )
Citation :

Structure of Ddn, the deazaflavin-dependent nitroreductase from Mycobacterium tuberculosis involved in bioreductive activation of PA-824.

Cellitti, S.E.,Shaffer, J.,Jones, D.H.  et al.
(2012)  Structure  20 : 101 - 112

PubMed: 22244759
DOI: 10.1016/j.str.2011.11.001

Chain : A, B, C, D, E
UniProt : P71854
Reaction : -