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Atomistry » Zinc » PDB 1ndw-1nvb » 1nkx » |
Zinc in PDB 1nkx: Crystal Structure of A Proteolytically Generated Functional Monoferric C-Lobe of Bovine Lactoferrin at 1.9A ResolutionProtein crystallography data
The structure of Crystal Structure of A Proteolytically Generated Functional Monoferric C-Lobe of Bovine Lactoferrin at 1.9A Resolution, PDB code: 1nkx
was solved by
S.Sharma,
J.Jasti,
J.Kumar,
A.K.Mohanty,
T.P.Singh,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1nkx:
The structure of Crystal Structure of A Proteolytically Generated Functional Monoferric C-Lobe of Bovine Lactoferrin at 1.9A Resolution also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of A Proteolytically Generated Functional Monoferric C-Lobe of Bovine Lactoferrin at 1.9A Resolution
(pdb code 1nkx). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of A Proteolytically Generated Functional Monoferric C-Lobe of Bovine Lactoferrin at 1.9A Resolution, PDB code: 1nkx: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 1nkxGo back to Zinc Binding Sites List in 1nkx
Zinc binding site 1 out
of 2 in the Crystal Structure of A Proteolytically Generated Functional Monoferric C-Lobe of Bovine Lactoferrin at 1.9A Resolution
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 1nkxGo back to Zinc Binding Sites List in 1nkx
Zinc binding site 2 out
of 2 in the Crystal Structure of A Proteolytically Generated Functional Monoferric C-Lobe of Bovine Lactoferrin at 1.9A Resolution
Mono view Stereo pair view
Reference:
S.Sharma,
J.Jasti,
J.Kumar,
A.K.Mohanty,
T.P.Singh.
Crystal Structure of A Proteolytically Generated Functional Monoferric C-Lobe of Bovine Lactoferrin at 1.9A Resolution J.Mol.Biol. V. 331 485 2003.
Page generated: Mon Jan 25 16:10:27 2021
ISSN: ISSN 0022-2836 PubMed: 12888354 DOI: 10.1016/S0022-2836(03)00717-4 |
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