Magnesium in PDB 2alf: Crystal Structure of Human Cypa Mutant K131A

All present enzymatic activity of Crystal Structure of Human Cypa Mutant K131A:
5.2.1.8;

The structure of Crystal Structure of Human Cypa Mutant K131A, PDB code: 2alf was solved by H.Hu, C.-Q.Huang, H.-L.Liu, Y.Han, M.-E.Chen, L.Yu, R.-C.Bi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.00 / 1.90
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	33.585, 68.264, 137.794, 90.00, 90.00, 90.00
R / Rfree (%)	19.3 / 22.6

The binding sites of Magnesium atom in the Crystal Structure of Human Cypa Mutant K131A (pdb code 2alf). 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 Human Cypa Mutant K131A, PDB code: 2alf:

Magnesium binding site 1 out of 1 in the Crystal Structure of Human Cypa Mutant K131A


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 Human Cypa Mutant K131A within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:20.0 occ:1.00 O A:HOH303 0.3 3.3 1.0 OG1 A:THR32 2.6 6.7 1.0 N A:GLU86 2.9 12.9 1.0 O A:GLU84 3.2 9.4 1.0 CG2 A:VAL127 3.4 7.6 1.0 CG1 A:VAL127 3.4 8.1 1.0 CB A:GLU86 3.5 10.9 1.0 CB A:VAL127 3.6 7.4 1.0 ND2 A:ASN108 3.7 9.5 1.0 CA A:ASP85 3.7 10.7 1.0 C A:ASP85 3.8 10.9 1.0 CA A:GLU86 3.8 11.0 1.0 CB A:THR32 3.9 8.0 1.0 CE2 A:PHE83 3.9 7.3 1.0 CG2 A:THR32 4.0 8.2 1.0 CG A:ASN108 4.2 9.8 1.0 C A:GLU84 4.2 11.1 1.0 N A:ASP85 4.4 11.5 1.0 OD1 A:ASN108 4.5 9.3 1.0 CD2 A:PHE83 4.5 9.4 1.0 OE1 A:GLU86 4.6 9.4 1.0 CZ A:PHE83 4.7 8.9 1.0 N A:ASN87 4.8 8.6 1.0 OD1 A:ASP85 4.8 10.7 1.0 CB A:ASP85 4.8 11.6 1.0 C A:GLU86 4.9 11.7 1.0 CG A:GLU86 4.9 9.8 1.0 CA A:THR32 4.9 8.5 1.0 CB A:ASN108 4.9 8.5 1.0 O A:ASP85 5.0 10.9 1.0

H.Hu, C.-Q.Huang, H.-L.Liu, Y.Han, M.-E.Chen, L.Yu, R.-C.Bi. Nuclease Activity of Cyclophilin A and Its Structural Basis To Be Published.