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Magnesium in PDB 4mnd: Crystal Structure of Archaeoglobus Fulgidus Ipct-Dipps Bifunctional Membrane Protein

Enzymatic activity of Crystal Structure of Archaeoglobus Fulgidus Ipct-Dipps Bifunctional Membrane Protein

All present enzymatic activity of Crystal Structure of Archaeoglobus Fulgidus Ipct-Dipps Bifunctional Membrane Protein:
2.7.7.74; 2.7.8.34;

Protein crystallography data

The structure of Crystal Structure of Archaeoglobus Fulgidus Ipct-Dipps Bifunctional Membrane Protein, PDB code: 4mnd was solved by P.Nogly, I.Gushchin, A.Remeeva, A.M.Esteves, A.Ishchenko, P.Ma, S.Grudinin, N.Borges, E.Round, I.Moraes, V.Borshchevskiy, H.Santos, V.Gordeliy, M.Archer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 53.85 / 2.66
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 41.369, 107.584, 123.953, 90.00, 90.00, 90.00
R / Rfree (%) 24.3 / 30

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Archaeoglobus Fulgidus Ipct-Dipps Bifunctional Membrane Protein (pdb code 4mnd). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Archaeoglobus Fulgidus Ipct-Dipps Bifunctional Membrane Protein, PDB code: 4mnd:

Magnesium binding site 1 out of 1 in 4mnd

Go back to Magnesium Binding Sites List in 4mnd
Magnesium binding site 1 out of 1 in the Crystal Structure of Archaeoglobus Fulgidus Ipct-Dipps Bifunctional Membrane Protein


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Archaeoglobus Fulgidus Ipct-Dipps Bifunctional Membrane Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg605

b:58.7
occ:1.00
OD2 A:ASP378 2.1 60.6 1.0
O A:ASP357 2.2 45.5 1.0
CG A:ASP378 2.9 51.5 1.0
OD1 A:ASP357 2.9 60.2 1.0
OD1 A:ASP378 3.0 52.9 1.0
OD2 A:ASP360 3.2 47.9 1.0
C A:ASP357 3.3 43.6 1.0
OD1 A:ASP360 3.5 51.2 1.0
CG A:ASP360 3.7 47.2 1.0
CG A:ASP357 3.8 57.9 1.0
CA A:ASP357 4.0 45.7 1.0
CB A:ASP357 4.1 53.3 1.0
OD2 A:ASP382 4.2 45.7 1.0
CB A:ASP378 4.4 45.8 1.0
N A:GLY358 4.4 42.1 1.0
CA A:GLY358 4.7 40.5 1.0
OD1 A:ASP382 4.7 39.6 1.0
OD2 A:ASP357 4.8 64.0 1.0
CG A:ASP382 4.9 40.3 1.0

Reference:

P.Nogly, I.Gushchin, A.Remeeva, A.M.Esteves, N.Borges, P.Ma, A.Ishchenko, S.Grudinin, E.Round, I.Moraes, V.Borshchevskiy, H.Santos, V.Gordeliy, M.Archer. X-Ray Structure of A Cdp-Alcohol Phosphatidyltransferase Membrane Enzyme and Insights Into Its Catalytic Mechanism. Nat Commun V. 5 4169 2014.
ISSN: ESSN 2041-1723
PubMed: 24942835
DOI: 10.1038/NCOMMS5169
Page generated: Mon Aug 19 23:15:42 2024

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