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Atomistry » Chlorine » PDB 4bjz-4brk » 4bmp » |
Chlorine in PDB 4bmp: Crystal Structure of Bacillus Cereus Ribonucleotide Reductase Di-Iron Nrdf in Complex with Nrdi (2.1 A Resolution)Enzymatic activity of Crystal Structure of Bacillus Cereus Ribonucleotide Reductase Di-Iron Nrdf in Complex with Nrdi (2.1 A Resolution)
All present enzymatic activity of Crystal Structure of Bacillus Cereus Ribonucleotide Reductase Di-Iron Nrdf in Complex with Nrdi (2.1 A Resolution):
1.17.4.1; Protein crystallography data
The structure of Crystal Structure of Bacillus Cereus Ribonucleotide Reductase Di-Iron Nrdf in Complex with Nrdi (2.1 A Resolution), PDB code: 4bmp
was solved by
M.Hammerstad,
H.-P.Hersleth,
A.K.Rohr,
K.K.Andersson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4bmp:
The structure of Crystal Structure of Bacillus Cereus Ribonucleotide Reductase Di-Iron Nrdf in Complex with Nrdi (2.1 A Resolution) also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Bacillus Cereus Ribonucleotide Reductase Di-Iron Nrdf in Complex with Nrdi (2.1 A Resolution)
(pdb code 4bmp). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Bacillus Cereus Ribonucleotide Reductase Di-Iron Nrdf in Complex with Nrdi (2.1 A Resolution), PDB code: 4bmp: Chlorine binding site 1 out of 1 in 4bmpGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Crystal Structure of Bacillus Cereus Ribonucleotide Reductase Di-Iron Nrdf in Complex with Nrdi (2.1 A Resolution)
![]() Mono view ![]() Stereo pair view
Reference:
M.Hammerstad,
H.Hersleth,
A.B.Tomter,
A.K.Rohr,
K.K.Andersson.
Crystal Structure of Bacillus Cereus Class Ib Ribonucleotide Reductase Di-Iron Nrdf in Complex with Nrdi. Acs Chem.Biol. V. 9 526 2014.
Page generated: Sun Jul 21 10:19:52 2024
ISSN: ISSN 1554-8929 PubMed: 24295378 DOI: 10.1021/CB400757H |
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