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Magnesium in PDB 3pug: Haloferax Volcanii Malate Synthase Native at 3MM Glyoxylate

Enzymatic activity of Haloferax Volcanii Malate Synthase Native at 3MM Glyoxylate

All present enzymatic activity of Haloferax Volcanii Malate Synthase Native at 3MM Glyoxylate:
2.3.3.9;

Protein crystallography data

The structure of Haloferax Volcanii Malate Synthase Native at 3MM Glyoxylate, PDB code: 3pug was solved by B.R.Howard, C.D.Bracken, A.M.Neighbor, G.C.Thomas, K.K.Lamlenn, H.L.Schubert, F.G.Whitby, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.70
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 156.370, 156.370, 141.455, 90.00, 90.00, 120.00
R / Rfree (%) 19.8 / 26.3

Other elements in 3pug:

The structure of Haloferax Volcanii Malate Synthase Native at 3MM Glyoxylate also contains other interesting chemical elements:

Potassium (K) 4 atoms
Chlorine (Cl) 4 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Haloferax Volcanii Malate Synthase Native at 3MM Glyoxylate (pdb code 3pug). 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 Haloferax Volcanii Malate Synthase Native at 3MM Glyoxylate, PDB code: 3pug:

Magnesium binding site 1 out of 1 in 3pug

Go back to Magnesium Binding Sites List in 3pug
Magnesium binding site 1 out of 1 in the Haloferax Volcanii Malate Synthase Native at 3MM Glyoxylate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Haloferax Volcanii Malate Synthase Native at 3MM Glyoxylate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg601

b:77.8
occ:1.00
O A:HOH476 2.0 56.0 1.0
OD2 A:ASP192 2.0 49.6 1.0
O1 A:GLV501 2.0 71.8 1.0
O3 A:GLV501 2.4 79.1 1.0
C1 A:GLV501 2.8 73.3 1.0
OE1 A:GLU158 2.9 41.0 1.0
CG A:ASP192 2.9 49.5 1.0
OD2 A:ASP52 3.0 53.5 1.0
C2 A:GLV501 3.0 74.5 1.0
O A:HOH485 3.1 46.0 1.0
CD A:GLU158 3.5 42.9 1.0
K A:K803 3.5 56.1 1.0
OE2 A:GLU158 3.5 42.0 1.0
CB A:ASP192 3.8 45.8 1.0
OD1 A:ASP192 3.8 55.9 1.0
CG A:ASP52 4.1 57.3 1.0
NH1 A:ARG84 4.2 60.0 1.0
O2 A:GLV501 4.2 75.0 1.0
OE1 A:GLU51 4.3 53.6 1.0
OE1 A:GLU123 4.3 43.2 1.0
N A:ASP192 4.6 44.9 1.0
OE2 A:GLU51 4.7 46.1 1.0
NH2 A:ARG84 4.8 54.3 1.0
CG A:GLU158 4.8 42.5 1.0
CA A:ASP192 4.8 44.0 1.0
CZ A:ARG84 4.9 55.8 1.0
OD1 A:ASP52 4.9 55.7 1.0
CB A:ASP52 4.9 57.7 1.0
CD A:GLU51 5.0 51.8 1.0

Reference:

C.D.Bracken, A.M.Neighbor, K.K.Lamlenn, G.C.Thomas, H.L.Schubert, F.G.Whitby, B.R.Howard. Crystal Structures of A Halophilic Archaeal Malate Synthase From Haloferax Volcanii and Comparisons with Isoforms A and G. Bmc Struct.Biol. V. 11 23 2011.
ISSN: ESSN 1472-6807
PubMed: 21569248
DOI: 10.1186/1472-6807-11-23
Page generated: Thu Aug 15 09:43:05 2024

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