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Atomistry » Chlorine » PDB 1cu6-1dhi » 1d3a | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 1cu6-1dhi » 1d3a » |
Chlorine in PDB 1d3a: Crystal Structure of the Wild Type Halophilic Malate Dehydrogenase in the Apo FormEnzymatic activity of Crystal Structure of the Wild Type Halophilic Malate Dehydrogenase in the Apo Form
All present enzymatic activity of Crystal Structure of the Wild Type Halophilic Malate Dehydrogenase in the Apo Form:
1.1.1.37; Protein crystallography data
The structure of Crystal Structure of the Wild Type Halophilic Malate Dehydrogenase in the Apo Form, PDB code: 1d3a
was solved by
S.B.Richard,
D.Madern,
E.Garcin,
G.Zaccai,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1d3a:
The structure of Crystal Structure of the Wild Type Halophilic Malate Dehydrogenase in the Apo Form also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of the Wild Type Halophilic Malate Dehydrogenase in the Apo Form
(pdb code 1d3a). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of the Wild Type Halophilic Malate Dehydrogenase in the Apo Form, PDB code: 1d3a: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 1d3aGo back to![]() ![]()
Chlorine binding site 1 out
of 2 in the Crystal Structure of the Wild Type Halophilic Malate Dehydrogenase in the Apo Form
![]() Mono view ![]() Stereo pair view
Chlorine binding site 2 out of 2 in 1d3aGo back to![]() ![]()
Chlorine binding site 2 out
of 2 in the Crystal Structure of the Wild Type Halophilic Malate Dehydrogenase in the Apo Form
![]() Mono view ![]() Stereo pair view
Reference:
S.B.Richard,
D.Madern,
E.Garcin,
G.Zaccai.
Halophilic Adaptation: Novel Solvent Protein Interactions Observed in the 2.9 and 2.6 A Resolution Structures of the Wild Type and A Mutant of Malate Dehydrogenase From Haloarcula Marismortui. Biochemistry V. 39 992 2000.
Page generated: Thu Jul 10 16:37:17 2025
ISSN: ISSN 0006-2960 PubMed: 10653643 DOI: 10.1021/BI991001A |
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