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Atomistry » Chlorine » PDB 2px4-2q6r » 2q0m | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 2px4-2q6r » 2q0m » |
Chlorine in PDB 2q0m: Tricarbonylmanganese(I)-Lysozyme Complex : A Structurally Characterized Organometallic ProteinEnzymatic activity of Tricarbonylmanganese(I)-Lysozyme Complex : A Structurally Characterized Organometallic Protein
All present enzymatic activity of Tricarbonylmanganese(I)-Lysozyme Complex : A Structurally Characterized Organometallic Protein:
3.2.1.17; Protein crystallography data
The structure of Tricarbonylmanganese(I)-Lysozyme Complex : A Structurally Characterized Organometallic Protein, PDB code: 2q0m
was solved by
M.Razavet,
V.Artero,
C.Cavazza,
Y.Oudart,
J.C.Fontecilla-Camps,
M.Fontecave,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2q0m:
The structure of Tricarbonylmanganese(I)-Lysozyme Complex : A Structurally Characterized Organometallic Protein also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Tricarbonylmanganese(I)-Lysozyme Complex : A Structurally Characterized Organometallic Protein
(pdb code 2q0m). 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 Tricarbonylmanganese(I)-Lysozyme Complex : A Structurally Characterized Organometallic Protein, PDB code: 2q0m: Chlorine binding site 1 out of 1 in 2q0mGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Tricarbonylmanganese(I)-Lysozyme Complex : A Structurally Characterized Organometallic Protein
![]() Mono view ![]() Stereo pair view
Reference:
M.Razavet,
V.Artero,
C.Cavazza,
Y.Oudart,
C.Lebrun,
J.C.Fontecilla-Camps,
M.Fontecave.
Tricarbonylmanganese(I)-Lysozyme Complex: A Structurally Characterized Organometallic Protein Chem.Commun.(Camb.) 2805 2007.
Page generated: Thu Jul 10 23:58:56 2025
ISSN: ESSN 1364-548X PubMed: 17609782 DOI: 10.1039/B703887A |
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