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Atomistry » Calcium » PDB 3hzb-3iit » 3ia7 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 3hzb-3iit » 3ia7 » |
Calcium in PDB 3ia7: Crystal Structure of CALG4, the Calicheamicin GlycosyltransferaseProtein crystallography data
The structure of Crystal Structure of CALG4, the Calicheamicin Glycosyltransferase, PDB code: 3ia7
was solved by
A.Chang,
S.Singh,
C.A.Bingman,
J.S.Thorson,
G.N.Phillips Jr.,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3ia7:
The structure of Crystal Structure of CALG4, the Calicheamicin Glycosyltransferase also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Crystal Structure of CALG4, the Calicheamicin Glycosyltransferase
(pdb code 3ia7). 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 CALG4, the Calicheamicin Glycosyltransferase, PDB code: 3ia7: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 3ia7Go back to Calcium Binding Sites List in 3ia7
Calcium binding site 1 out
of 2 in the Crystal Structure of CALG4, the Calicheamicin Glycosyltransferase
Mono view Stereo pair view
Calcium binding site 2 out of 2 in 3ia7Go back to Calcium Binding Sites List in 3ia7
Calcium binding site 2 out
of 2 in the Crystal Structure of CALG4, the Calicheamicin Glycosyltransferase
Mono view Stereo pair view
Reference:
A.Chang,
S.Singh,
K.E.Helmich,
R.D.Goff,
C.A.Bingman,
J.S.Thorson,
G.N.Phillips.
Complete Set of Glycosyltransferase Structures in the Calicheamicin Biosynthetic Pathway Reveals the Origin of Regiospecificity. Proc.Natl.Acad.Sci.Usa V. 108 17649 2011.
Page generated: Sat Dec 12 04:15:13 2020
ISSN: ISSN 0027-8424 PubMed: 21987796 DOI: 10.1073/PNAS.1108484108 |
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