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Atomistry » Calcium » PDB 5b4y-5bx5 » 5b72 » |
Calcium in PDB 5b72: Crystal Structure of Bovine Lactoperoxidase with A Broken Covalent Bond Between GLU258 and Heme Moiety at 1.98 A Resolution.Enzymatic activity of Crystal Structure of Bovine Lactoperoxidase with A Broken Covalent Bond Between GLU258 and Heme Moiety at 1.98 A Resolution.
All present enzymatic activity of Crystal Structure of Bovine Lactoperoxidase with A Broken Covalent Bond Between GLU258 and Heme Moiety at 1.98 A Resolution.:
1.11.1.7; Protein crystallography data
The structure of Crystal Structure of Bovine Lactoperoxidase with A Broken Covalent Bond Between GLU258 and Heme Moiety at 1.98 A Resolution., PDB code: 5b72
was solved by
P.K.Singh,
H.V.Sirohi,
P.Kaur,
S.Sharma,
T.P.Singh,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5b72:
The structure of Crystal Structure of Bovine Lactoperoxidase with A Broken Covalent Bond Between GLU258 and Heme Moiety at 1.98 A Resolution. also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Crystal Structure of Bovine Lactoperoxidase with A Broken Covalent Bond Between GLU258 and Heme Moiety at 1.98 A Resolution.
(pdb code 5b72). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of Bovine Lactoperoxidase with A Broken Covalent Bond Between GLU258 and Heme Moiety at 1.98 A Resolution., PDB code: 5b72: Calcium binding site 1 out of 1 in 5b72Go back to Calcium Binding Sites List in 5b72
Calcium binding site 1 out
of 1 in the Crystal Structure of Bovine Lactoperoxidase with A Broken Covalent Bond Between GLU258 and Heme Moiety at 1.98 A Resolution.
Mono view Stereo pair view
Reference:
P.K.Singh,
H.V.Sirohi,
N.Iqbal,
P.Tiwari,
P.Kaur,
S.Sharma,
T.P.Singh.
Structure of Bovine Lactoperoxidase with A Partially Linked Heme Moiety at 1.98 Angstrom Resolution Biochim. Biophys. Acta V.1865 329 2016.
Page generated: Sun Jul 14 16:51:02 2024
ISSN: ISSN 0006-3002 PubMed: 27986533 DOI: 10.1016/J.BBAPAP.2016.12.006 |
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