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Magnesium in PDB 3oyz: Haloferax Volcanii Malate Synthase Pyruvate/Acetyl-Coa Ternary Complex

Enzymatic activity of Haloferax Volcanii Malate Synthase Pyruvate/Acetyl-Coa Ternary Complex

All present enzymatic activity of Haloferax Volcanii Malate Synthase Pyruvate/Acetyl-Coa Ternary Complex:
2.3.3.9;

Protein crystallography data

The structure of Haloferax Volcanii Malate Synthase Pyruvate/Acetyl-Coa Ternary Complex, PDB code: 3oyz was solved by B.R.Howard, C.Bracken, A.Neighbor, G.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 / 1.95
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 154.788, 154.788, 142.144, 90.00, 90.00, 120.00
R / Rfree (%) 20.3 / 23.9

Other elements in 3oyz:

The structure of Haloferax Volcanii Malate Synthase Pyruvate/Acetyl-Coa Ternary Complex also contains other interesting chemical elements:

Potassium (K) 3 atoms
Chlorine (Cl) 4 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Haloferax Volcanii Malate Synthase Pyruvate/Acetyl-Coa Ternary Complex (pdb code 3oyz). 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 Pyruvate/Acetyl-Coa Ternary Complex, PDB code: 3oyz:

Magnesium binding site 1 out of 1 in 3oyz

Go back to Magnesium Binding Sites List in 3oyz
Magnesium binding site 1 out of 1 in the Haloferax Volcanii Malate Synthase Pyruvate/Acetyl-Coa Ternary Complex


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 Pyruvate/Acetyl-Coa Ternary Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg500

b:32.1
occ:1.00
 OD2 A:ASP192 1.9 37.8 1.0
O1 A:PYR435 1.9 39.4 1.0
O A:HOH471 2.0 42.3 1.0
OE2 A:GLU158 2.1 34.8 1.0
O3 A:PYR435 2.2 46.9 1.0
O A:HOH498 2.4 45.2 1.0
C1 A:PYR435 2.8 38.2 1.0
C2 A:PYR435 2.8 48.5 1.0
CG A:ASP192 2.9 39.2 1.0
CD A:GLU158 3.0 36.8 1.0
CB A:ASP192 3.3 32.6 1.0
OE1 A:GLU158 3.4 32.0 1.0
O A:HOH440 3.8 43.5 1.0
O2 A:PYR435 4.0 34.5 1.0
OD1 A:ASP192 4.0 39.7 1.0
CH3 A:ACO434 4.2 48.6 1.0
NH1 A:ARG84 4.2 35.1 1.0
N A:ASP192 4.3 32.1 1.0
C3 A:PYR435 4.3 49.9 1.0
O A:ACO434 4.3 50.0 1.0
CB A:ALA390 4.4 39.8 1.0
OD2 A:ASP52 4.4 57.5 1.0
CG A:GLU158 4.4 32.5 1.0
CA A:ASP192 4.4 31.3 1.0
OE1 A:GLU123 4.5 39.4 1.0
OE1 A:GLU51 4.5 42.3 1.0
CB A:GLU158 4.7 32.6 1.0
C A:ACO434 4.7 49.6 1.0
OE2 A:GLU51 4.8 38.4 1.0
O A:HOH537 5.0 55.0 1.0
CG2 A:ILE156 5.0 28.1 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 08:59:24 2024

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