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Atomistry » Sodium » PDB 1nnh-1oan » 1no5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 1nnh-1oan » 1no5 » |
Sodium in PDB 1no5: Structure of HI0073 From Haemophilus Influenzae, the Nucleotide Binding Domain of the HI0073/HI0074 Two Protein Nucleotidyl Transferase.Protein crystallography data
The structure of Structure of HI0073 From Haemophilus Influenzae, the Nucleotide Binding Domain of the HI0073/HI0074 Two Protein Nucleotidyl Transferase., PDB code: 1no5
was solved by
C.Lehmann,
S.Pullalarevu,
A.Galkin,
W.Krajewski,
M.A.Willis,
A.Howard,
O.Herzberg,
Structure 2 Function Project (S2F),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1no5:
The structure of Structure of HI0073 From Haemophilus Influenzae, the Nucleotide Binding Domain of the HI0073/HI0074 Two Protein Nucleotidyl Transferase. also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Structure of HI0073 From Haemophilus Influenzae, the Nucleotide Binding Domain of the HI0073/HI0074 Two Protein Nucleotidyl Transferase.
(pdb code 1no5). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Structure of HI0073 From Haemophilus Influenzae, the Nucleotide Binding Domain of the HI0073/HI0074 Two Protein Nucleotidyl Transferase., PDB code: 1no5: Sodium binding site 1 out of 1 in 1no5Go back to![]() ![]()
Sodium binding site 1 out
of 1 in the Structure of HI0073 From Haemophilus Influenzae, the Nucleotide Binding Domain of the HI0073/HI0074 Two Protein Nucleotidyl Transferase.
![]() Mono view ![]() Stereo pair view
Reference:
C.Lehmann,
S.Pullalarevu,
W.Krajewski,
M.A.Willis,
A.Galkin,
A.Howard,
O.Herzberg.
Structure of HI0073 From Haemophilus Influenzae, the Nucleotide-Binding Domain of A Two-Protein Nucleotidyl Transferase Proteins V. 60 807 2005.
Page generated: Sun Oct 6 20:59:58 2024
ISSN: ISSN 0887-3585 PubMed: 16028221 DOI: 10.1002/PROT.20586 |
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