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Atomistry » Zinc » PDB 1xv2-1y8j » 1xxw » |
Zinc in PDB 1xxw: Structure of Zinc Induced Heterodimer of Two Calcium Free Isoforms of Phospholipase A2 From Naja Naja Sagittifera at 2.7A ResolutionEnzymatic activity of Structure of Zinc Induced Heterodimer of Two Calcium Free Isoforms of Phospholipase A2 From Naja Naja Sagittifera at 2.7A Resolution
All present enzymatic activity of Structure of Zinc Induced Heterodimer of Two Calcium Free Isoforms of Phospholipase A2 From Naja Naja Sagittifera at 2.7A Resolution:
3.1.1.4; Protein crystallography data
The structure of Structure of Zinc Induced Heterodimer of Two Calcium Free Isoforms of Phospholipase A2 From Naja Naja Sagittifera at 2.7A Resolution, PDB code: 1xxw
was solved by
T.Jabeen,
S.Sharma,
N.Singh,
R.K.Singh,
A.K.Verma,
M.Paramasivam,
A.Srinivasan,
T.P.Singh,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Zinc Binding Sites:
The binding sites of Zinc atom in the Structure of Zinc Induced Heterodimer of Two Calcium Free Isoforms of Phospholipase A2 From Naja Naja Sagittifera at 2.7A Resolution
(pdb code 1xxw). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Structure of Zinc Induced Heterodimer of Two Calcium Free Isoforms of Phospholipase A2 From Naja Naja Sagittifera at 2.7A Resolution, PDB code: 1xxw: Zinc binding site 1 out of 1 in 1xxwGo back to![]() ![]()
Zinc binding site 1 out
of 1 in the Structure of Zinc Induced Heterodimer of Two Calcium Free Isoforms of Phospholipase A2 From Naja Naja Sagittifera at 2.7A Resolution
![]() Mono view ![]() Stereo pair view
Reference:
T.Jabeen,
S.Sharma,
N.Singh,
R.K.Singh,
A.K.Verma,
M.Paramasivam,
A.Srinivasan,
T.P.Singh.
Structure of the Zinc-Induced Heterodimer of Two Calcium-Free Isoforms of Phospholipase A2 From Naja Naja Sagittifera at 2.7 Angstroms Resolution. Acta Crystallogr.,Sect.D V. 61 302 2005.
Page generated: Wed Oct 16 20:39:57 2024
ISSN: ISSN 0907-4449 PubMed: 15735340 DOI: 10.1107/S0907444904033165 |
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