Magnesium in PDB 2wfi: Atomic Resolution Crystal Structure of the Ppiase Domain of Human Cyclophilin G

All present enzymatic activity of Atomic Resolution Crystal Structure of the Ppiase Domain of Human Cyclophilin G:
5.2.1.8;

The structure of Atomic Resolution Crystal Structure of the Ppiase Domain of Human Cyclophilin G, PDB code: 2wfi was solved by C.M.Stegmann, G.M.Sheldrick, M.C.Wahl, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 0.75
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	37.544, 65.144, 69.680, 90.00, 90.00, 90.00
R / Rfree (%)	10.7 / 12.4

The binding sites of Magnesium atom in the Atomic Resolution Crystal Structure of the Ppiase Domain of Human Cyclophilin G (pdb code 2wfi). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Atomic Resolution Crystal Structure of the Ppiase Domain of Human Cyclophilin G, PDB code: 2wfi:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Atomic Resolution Crystal Structure of the Ppiase Domain of Human Cyclophilin G


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Atomic Resolution Crystal Structure of the Ppiase Domain of Human Cyclophilin G within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1001 b:7.6 occ:0.95 O A:HOH2322 2.0 11.6 1.0 O A:HOH2268 2.1 10.2 1.0 O A:HOH2323 2.1 7.7 1.0 O A:ASP97 4.1 7.5 1.0 O A:HOH2109 4.2 11.3 1.0 O A:HOH2110 4.2 26.9 1.0 OE2 A:GLU96 4.2 18.1 0.5 OD1 A:ASP118 4.3 7.8 1.0 OD2 A:ASP118 4.4 12.2 1.0 OE1 A:GLU96 4.5 17.0 0.5 O A:HOH2278 4.5 9.3 1.0 O A:HOH2320 4.5 10.9 1.0 O A:HOH2277 4.6 13.6 1.0 CB A:GLU96 4.6 8.3 0.5 CB A:GLU96 4.8 6.5 0.5 CG A:ASP118 4.8 8.4 1.0 CG A:GLU96 4.9 9.2 0.5 O A:HOH2273 4.9 14.7 1.0 CD A:GLU96 5.0 12.2 0.5

Magnesium binding site 2 out of 2 in the Atomic Resolution Crystal Structure of the Ppiase Domain of Human Cyclophilin G


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Atomic Resolution Crystal Structure of the Ppiase Domain of Human Cyclophilin G within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1002 b:9.5 occ:0.22 O A:HOH2309 1.9 21.5 1.0 O A:HOH2125 2.0 13.6 0.2 O A:HOH2308 2.0 15.4 0.5 O A:HOH2349 2.1 18.8 1.0 O A:HOH2348 2.1 11.1 0.2 O A:HOH2316 2.2 32.6 1.0 O A:HOH2346 3.2 27.9 1.0 O A:HOH2147 3.8 41.3 1.0 O A:HOH2321 3.8 23.4 0.5 O A:HOH2307 3.9 22.1 0.5 OD1 A:ASN114 4.0 8.0 1.0 NE2 A:HIS138 4.2 7.9 1.0 N A:GLY116 4.6 8.9 1.0 CE1 A:HIS138 4.6 7.2 1.0 ND1 A:HIS137 4.7 9.6 1.0 CA A:GLY116 4.8 10.5 1.0 CB A:HIS137 4.9 7.0 1.0

C.M.Stegmann, D.Seeliger, G.M.Sheldrick, B.L.De Groot, M.C.Wahl. The Thermodynamic Influence of Trapped Water Molecules on A Protein-Ligand Interaction Angew.Chem.Int.Ed.Engl. V. 48 5207 2009.
ISSN: ISSN 1433-7851
PubMed: 19499554
DOI: 10.1002/ANIE.200900481