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Atomistry » Sodium » PDB 4jvl-4khs » 4k6a » |
Sodium in PDB 4k6a: Revised Crystal Structure of Apo-Form of Triosephosphate Isomerase (Tpia) From Escherichia Coli at 1.8 Angstrom Resolution.Enzymatic activity of Revised Crystal Structure of Apo-Form of Triosephosphate Isomerase (Tpia) From Escherichia Coli at 1.8 Angstrom Resolution.
All present enzymatic activity of Revised Crystal Structure of Apo-Form of Triosephosphate Isomerase (Tpia) From Escherichia Coli at 1.8 Angstrom Resolution.:
5.3.1.1; Protein crystallography data
The structure of Revised Crystal Structure of Apo-Form of Triosephosphate Isomerase (Tpia) From Escherichia Coli at 1.8 Angstrom Resolution., PDB code: 4k6a
was solved by
G.Minasov,
M.Kuhn,
A.Halavaty,
L.Shuvalova,
I.Dubrovska,
J.Winsor,
S.Grimshaw,
W.F.Anderson,
Center For Structural Genomics Of Infectiousdiseases (Csgid),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Sodium Binding Sites:
The binding sites of Sodium atom in the Revised Crystal Structure of Apo-Form of Triosephosphate Isomerase (Tpia) From Escherichia Coli at 1.8 Angstrom Resolution.
(pdb code 4k6a). 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 Revised Crystal Structure of Apo-Form of Triosephosphate Isomerase (Tpia) From Escherichia Coli at 1.8 Angstrom Resolution., PDB code: 4k6a: Sodium binding site 1 out of 1 in 4k6aGo back to![]() ![]()
Sodium binding site 1 out
of 1 in the Revised Crystal Structure of Apo-Form of Triosephosphate Isomerase (Tpia) From Escherichia Coli at 1.8 Angstrom Resolution.
![]() Mono view ![]() Stereo pair view
Reference:
M.L.Kuhn,
B.Zemaitaitis,
L.I.Hu,
A.Sahu,
D.Sorensen,
G.Minasov,
B.P.Lima,
M.Scholle,
M.Mrksich,
W.F.Anderson,
B.W.Gibson,
B.Schilling,
A.J.Wolfe.
Structural, Kinetic and Proteomic Characterization of Acetyl Phosphate-Dependent Bacterial Protein Acetylation. Plos One V. 9 94816 2014.
Page generated: Sun Aug 17 20:09:36 2025
ISSN: ESSN 1932-6203 PubMed: 24756028 DOI: 10.1371/JOURNAL.PONE.0094816 |
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