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Atomistry » Sodium » PDB 5hn3-5i9b » 5i3k » |
Sodium in PDB 5i3k: Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate IsomeraseEnzymatic activity of Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase
All present enzymatic activity of Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase:
5.3.1.1; Protein crystallography data
The structure of Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase, PDB code: 5i3k
was solved by
E.J.Drake,
A.M.Gulick,
J.P.Richard,
X.Zhai,
K.Kim,
C.J.Reinhardt,
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 Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase
(pdb code 5i3k). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 3 binding sites of Sodium where determined in the Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase, PDB code: 5i3k: Jump to Sodium binding site number: 1; 2; 3; Sodium binding site 1 out of 3 in 5i3kGo back to Sodium Binding Sites List in 5i3k
Sodium binding site 1 out
of 3 in the Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase
Mono view Stereo pair view
Sodium binding site 2 out of 3 in 5i3kGo back to Sodium Binding Sites List in 5i3k
Sodium binding site 2 out
of 3 in the Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase
Mono view Stereo pair view
Sodium binding site 3 out of 3 in 5i3kGo back to Sodium Binding Sites List in 5i3k
Sodium binding site 3 out
of 3 in the Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase
Mono view Stereo pair view
Reference:
J.P.Richard,
T.L.Amyes,
M.M.Malabanan,
X.Zhai,
K.J.Kim,
C.J.Reinhardt,
R.K.Wierenga,
E.J.Drake,
A.M.Gulick.
Structure-Function Studies of Hydrophobic Residues That Clamp A Basic Glutamate Side Chain During Catalysis By Triosephosphate Isomerase. Biochemistry V. 55 3036 2016.
Page generated: Mon Oct 7 21:31:24 2024
ISSN: ISSN 0006-2960 PubMed: 27149328 DOI: 10.1021/ACS.BIOCHEM.6B00311 |
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