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Magnesium in PDB 2dua: Crystal Structure of Phosphonopyruvate Hydrolase Complex with Oxalate and Mg++

Protein crystallography data

The structure of Crystal Structure of Phosphonopyruvate Hydrolase Complex with Oxalate and Mg++, PDB code: 2dua was solved by O.Herzberg, C.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.78 / 2.00
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 74.890, 79.180, 93.430, 90.00, 90.00, 90.00
R / Rfree (%) 15.6 / 21.9

Other elements in 2dua:

The structure of Crystal Structure of Phosphonopyruvate Hydrolase Complex with Oxalate and Mg++ also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms
Sodium (Na) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Phosphonopyruvate Hydrolase Complex with Oxalate and Mg++ (pdb code 2dua). 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 Phosphonopyruvate Hydrolase Complex with Oxalate and Mg++, PDB code: 2dua:

Magnesium binding site 1 out of 1 in 2dua

Go back to Magnesium Binding Sites List in 2dua
Magnesium binding site 1 out of 1 in the Crystal Structure of Phosphonopyruvate Hydrolase Complex with Oxalate and Mg++


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 Phosphonopyruvate Hydrolase Complex with Oxalate and Mg++ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg292

b:22.6
occ:1.00
O3 A:OXL291 2.1 19.7 1.0
OD2 A:ASP81 2.1 12.0 1.0
O A:HOH301 2.1 15.6 1.0
O2 A:OXL291 2.2 24.5 1.0
O A:HOH303 2.2 16.1 1.0
O A:HOH302 2.3 20.6 1.0
C1 A:OXL291 2.8 23.2 1.0
C2 A:OXL291 2.9 23.7 1.0
CG A:ASP81 3.1 11.4 1.0
OD1 A:ASP81 3.5 11.0 1.0
O A:HOH604 3.8 39.9 1.0
N A:PHE44 3.8 11.3 1.0
OD2 A:ASP83 3.9 28.7 1.0
N A:GLY43 3.9 9.3 1.0
OD1 A:ASP54 4.0 17.5 1.0
O1 A:OXL291 4.1 19.9 1.0
O4 A:OXL291 4.1 25.0 1.0
O A:HOH406 4.1 24.1 1.0
CA A:GLY43 4.2 11.2 1.0
CB A:ASP81 4.4 11.1 1.0
OD2 A:ASP54 4.4 17.6 1.0
C A:GLY43 4.4 10.8 1.0
CB A:PHE44 4.6 12.6 1.0
CG A:ASP54 4.6 17.5 1.0
CZ2 A:TRP40 4.7 8.7 1.0
CA A:PHE44 4.8 10.7 1.0
O A:HOH341 4.9 16.6 1.0
CG A:ASP83 5.0 26.1 1.0
O A:HOH573 5.0 52.4 1.0

Reference:

C.C.H.Chen, Y.Han, W.Niu, A.N.Kulakova, A.Howard, J.P.Quinn, D.Dunaway-Mariano, O.Herzberg. Structure and Kinetics of Phosphonopyruvate Hydrolase From Voriovorax Sp. PAL2: New Insight Into the Divergence of Catalysis Within the Pep Mutase/Isocitrate Lyase Superfamily Biochemistry V. 45 11491 2006.
ISSN: ISSN 0006-2960
PubMed: 16981709
DOI: 10.1021/BI061208L
Page generated: Mon Dec 14 07:20:37 2020

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