Magnesium in PDB 1p8f: A Four Location Model to Explain the Stereospecificity of Proteins.

All present enzymatic activity of A Four Location Model to Explain the Stereospecificity of Proteins.:
1.1.1.42;

The structure of A Four Location Model to Explain the Stereospecificity of Proteins., PDB code: 1p8f was solved by A.D.Mesecar, D.E.Koshland Jr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.86 / 1.85
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	103.306, 103.306, 150.004, 90.00, 90.00, 90.00
R / Rfree (%)	19.2 / 22.5

The binding sites of Magnesium atom in the A Four Location Model to Explain the Stereospecificity of Proteins. (pdb code 1p8f). 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 A Four Location Model to Explain the Stereospecificity of Proteins., PDB code: 1p8f:

Magnesium binding site 1 out of 1 in the A Four Location Model to Explain the Stereospecificity of Proteins.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of A Four Location Model to Explain the Stereospecificity of Proteins. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg420 b:18.7 occ:1.00 OD1 A:ASP307 2.0 13.4 1.0 O7 A:ICT601 2.1 17.2 1.0 O A:HOH802 2.1 17.9 1.0 O2 A:ICT601 2.2 18.4 1.0 C1 A:ICT601 3.0 21.1 1.0 C2 A:ICT601 3.0 17.7 1.0 CG A:ASP307 3.1 17.7 1.0 OD2 A:ASP307 3.6 18.8 1.0 OD1 A:ASP311 3.9 24.2 1.0 C6 A:ICT601 4.1 21.2 1.0 O1 A:ICT601 4.2 22.8 1.0 C3 A:ICT601 4.2 19.4 1.0 O A:ASP307 4.2 14.1 1.0 NH1 A:ARG129 4.2 18.8 1.0 O A:HOH976 4.3 31.1 1.0 O A:HOH837 4.3 23.4 1.0 O5 A:ICT601 4.3 21.6 1.0 O6 A:ICT601 4.3 20.0 1.0 CB A:ASP307 4.3 15.8 1.0 CG A:ASP311 4.4 22.8 1.0 OD2 A:ASP311 4.5 19.8 1.0 CA A:ASP307 4.6 12.7 1.0 C A:ASP307 4.7 13.7 1.0 NH1 A:ARG153 4.8 14.0 1.0

A.D.Mesecar, D.E.Koshland Jr.. Structural Biology: A New Model For Protein Stereospecificity. Nature V. 403 614 2000.
ISSN: ISSN 0028-0836
PubMed: 10688187