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Atomistry » Sodium » PDB 7opz-7pfg » 7pf7 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 7opz-7pfg » 7pf7 » |
Sodium in PDB 7pf7: Apo Structure of Synftn Variant D65AEnzymatic activity of Apo Structure of Synftn Variant D65A
All present enzymatic activity of Apo Structure of Synftn Variant D65A:
1.16.3.2; Protein crystallography data
The structure of Apo Structure of Synftn Variant D65A, PDB code: 7pf7
was solved by
A.M.Hemmings,
J.M.Bradley,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 7pf7:
The structure of Apo Structure of Synftn Variant D65A also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Apo Structure of Synftn Variant D65A
(pdb code 7pf7). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 3 binding sites of Sodium where determined in the Apo Structure of Synftn Variant D65A, PDB code: 7pf7: Jump to Sodium binding site number: 1; 2; 3; Sodium binding site 1 out of 3 in 7pf7Go back to Sodium Binding Sites List in 7pf7
Sodium binding site 1 out
of 3 in the Apo Structure of Synftn Variant D65A
Mono view Stereo pair view
Sodium binding site 2 out of 3 in 7pf7Go back to Sodium Binding Sites List in 7pf7
Sodium binding site 2 out
of 3 in the Apo Structure of Synftn Variant D65A
Mono view Stereo pair view
Sodium binding site 3 out of 3 in 7pf7Go back to Sodium Binding Sites List in 7pf7
Sodium binding site 3 out
of 3 in the Apo Structure of Synftn Variant D65A
Mono view Stereo pair view
Reference:
J.M.Bradley,
J.Fair,
A.M.Hemmings,
N.E.Le Brun.
Key Carboxylate Residues For Iron Transit Through the Prokaryotic Ferritin Syn Ftn. Microbiology (Reading, V. 167 2021ENGL.).
Page generated: Tue Oct 8 18:29:19 2024
ISSN: ESSN 1465-2080 PubMed: 34825885 DOI: 10.1099/MIC.0.001105 |
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