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Atomistry » Magnesium » PDB 3e3z-3ef8 » 3ebg | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 3e3z-3ef8 » 3ebg » |
Magnesium in PDB 3ebg: Structure of the M1 Alanylaminopeptidase From MalariaProtein crystallography data
The structure of Structure of the M1 Alanylaminopeptidase From Malaria, PDB code: 3ebg
was solved by
S.Mcgowan,
C.J.Porter,
A.M.Buckle,
J.C.Whisstock,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3ebg:
The structure of Structure of the M1 Alanylaminopeptidase From Malaria also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Structure of the M1 Alanylaminopeptidase From Malaria
(pdb code 3ebg). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of the M1 Alanylaminopeptidase From Malaria, PDB code: 3ebg: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 3ebgGo back to![]() ![]()
Magnesium binding site 1 out
of 2 in the Structure of the M1 Alanylaminopeptidase From Malaria
![]() Mono view ![]() Stereo pair view
Magnesium binding site 2 out of 2 in 3ebgGo back to![]() ![]()
Magnesium binding site 2 out
of 2 in the Structure of the M1 Alanylaminopeptidase From Malaria
![]() Mono view ![]() Stereo pair view
Reference:
S.Mcgowan,
C.J.Porter,
J.Lowther,
C.M.Stack,
S.J.Golding,
T.S.Skinner-Adams,
K.R.Trenholme,
F.Teuscher,
S.M.Donnelly,
J.Grembecka,
A.Mucha,
P.Kafarski,
R.Degori,
A.M.Buckle,
D.L.Gardiner,
J.C.Whisstock,
J.P.Dalton.
Structural Basis For the Inhibition of the Essential Plasmodium Falciparum M1 Neutral Aminopeptidase Proc.Natl.Acad.Sci.Usa V. 106 2537 2009.
Page generated: Wed Aug 14 12:59:37 2024
ISSN: ISSN 0027-8424 PubMed: 19196988 DOI: 10.1073/PNAS.0807398106 |
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