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Atomistry » Iron » PDB 1eb7-1esz » 1ep3 » |
Iron in PDB 1ep3: Crystal Structure of Lactococcus Lactis Dihydroorotate Dehydrogenase B. Data Collected Under Cryogenic Conditions.Enzymatic activity of Crystal Structure of Lactococcus Lactis Dihydroorotate Dehydrogenase B. Data Collected Under Cryogenic Conditions.
All present enzymatic activity of Crystal Structure of Lactococcus Lactis Dihydroorotate Dehydrogenase B. Data Collected Under Cryogenic Conditions.:
1.3.3.1; Protein crystallography data
The structure of Crystal Structure of Lactococcus Lactis Dihydroorotate Dehydrogenase B. Data Collected Under Cryogenic Conditions., PDB code: 1ep3
was solved by
P.Rowland,
S.Norager,
K.F.Jensen,
S.Larsen,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Iron Binding Sites:
The binding sites of Iron atom in the Crystal Structure of Lactococcus Lactis Dihydroorotate Dehydrogenase B. Data Collected Under Cryogenic Conditions.
(pdb code 1ep3). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Lactococcus Lactis Dihydroorotate Dehydrogenase B. Data Collected Under Cryogenic Conditions., PDB code: 1ep3: Jump to Iron binding site number: 1; 2; Iron binding site 1 out of 2 in 1ep3Go back to![]() ![]()
Iron binding site 1 out
of 2 in the Crystal Structure of Lactococcus Lactis Dihydroorotate Dehydrogenase B. Data Collected Under Cryogenic Conditions.
![]() Mono view ![]() Stereo pair view
Iron binding site 2 out of 2 in 1ep3Go back to![]() ![]()
Iron binding site 2 out
of 2 in the Crystal Structure of Lactococcus Lactis Dihydroorotate Dehydrogenase B. Data Collected Under Cryogenic Conditions.
![]() Mono view ![]() Stereo pair view
Reference:
P.Rowland,
S.Norager,
K.F.Jensen,
S.Larsen.
Structure of Dihydroorotate Dehydrogenase B: Electron Transfer Between Two Flavin Groups Bridged By An Iron-Sulphur Cluster. Structure Fold.Des. V. 8 1227 2000.
Page generated: Wed Jul 16 13:50:20 2025
ISSN: ISSN 0969-2126 PubMed: 11188687 DOI: 10.1016/S0969-2126(00)00530-X |
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