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Atomistry » Calcium » PDB 4wnb-4x8d » 4wpa » |
Calcium in PDB 4wpa: Crystal Structure of Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to Pyrophosphate and CalciumEnzymatic activity of Crystal Structure of Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to Pyrophosphate and Calcium
All present enzymatic activity of Crystal Structure of Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to Pyrophosphate and Calcium:
4.6.1.1; Protein crystallography data
The structure of Crystal Structure of Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to Pyrophosphate and Calcium, PDB code: 4wpa
was solved by
N.G.Bharambe,
D.V.Barathy,
K.Suguna,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Calcium Binding Sites:
The binding sites of Calcium atom in the Crystal Structure of Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to Pyrophosphate and Calcium
(pdb code 4wpa). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to Pyrophosphate and Calcium, PDB code: 4wpa: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 4wpaGo back to Calcium Binding Sites List in 4wpa
Calcium binding site 1 out
of 2 in the Crystal Structure of Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to Pyrophosphate and Calcium
Mono view Stereo pair view
Calcium binding site 2 out of 2 in 4wpaGo back to Calcium Binding Sites List in 4wpa
Calcium binding site 2 out
of 2 in the Crystal Structure of Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to Pyrophosphate and Calcium
Mono view Stereo pair view
Reference:
D.V.Barathy,
N.G.Bharambe,
W.Syed,
A.Zaveri,
S.S.Visweswariah,
M.Cola Sigmaf O,
S.Misquith,
K.Suguna.
Autoinhibitory Mechanism and Activity-Related Structural Changes in A Mycobacterial Adenylyl Cyclase J.Struct.Biol. V. 190 304 2015.
Page generated: Sat Dec 12 05:11:11 2020
ISSN: ESSN 1095-8657 PubMed: 25916753 DOI: 10.1016/J.JSB.2015.04.013 |
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