Magnesium in PDB 8t7p: X-Ray Crystal Structure of Pfa-M1(M462S)

The structure of X-Ray Crystal Structure of Pfa-M1(M462S), PDB code: 8t7p was solved by W.Yang, N.Drinkwater, C.T.Webb, S.Mcgowan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.37 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	75.01, 108.93, 117.63, 90, 90, 90
R / Rfree (%)	20.5 / 24.3

The structure of X-Ray Crystal Structure of Pfa-M1(M462S) also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Magnesium atom in the X-Ray Crystal Structure of Pfa-M1(M462S) (pdb code 8t7p). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the X-Ray Crystal Structure of Pfa-M1(M462S), PDB code: 8t7p:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the X-Ray Crystal Structure of Pfa-M1(M462S)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of X-Ray Crystal Structure of Pfa-M1(M462S) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1107 b:27.8 occ:1.00 O A:HOH1759 2.1 23.6 1.0 O A:GLY250 2.1 21.9 1.0 O A:HOH1488 2.1 25.9 1.0 O A:HOH1465 2.2 17.2 1.0 O A:HOH1645 2.3 34.5 1.0 C A:GLY250 3.1 21.4 1.0 CA A:GLY250 3.7 21.0 1.0 O A:HOH1408 4.1 16.7 1.0 N A:LEU251 4.3 21.4 1.0 O A:HOH1741 4.3 16.5 1.0 O A:HOH1485 4.5 37.2 1.0 ND1 A:HIS297 4.5 20.8 1.0 O A:ILE295 4.6 19.6 1.0 CA A:LEU251 4.7 21.4 1.0 CA A:ILE296 4.9 18.0 1.0

Magnesium binding site 2 out of 2 in the X-Ray Crystal Structure of Pfa-M1(M462S)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of X-Ray Crystal Structure of Pfa-M1(M462S) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1108 b:39.4 occ:1.00 O A:HOH1308 2.1 46.0 1.0 O A:HOH1704 2.1 43.5 1.0 O A:HOH1431 2.1 24.5 1.0 O A:HOH1369 2.1 23.7 1.0 O A:HOH1285 2.2 26.9 1.0 O A:HOH1424 2.3 25.8 1.0 ZN A:ZN1101 3.4 20.2 1.0 O A:HOH1714 3.5 47.8 1.0 OH A:TYR580 3.6 18.9 1.0 O A:HOH1798 3.6 30.0 1.0 OE1 A:GLU463 3.9 23.3 1.0 O A:HOH1799 3.9 37.2 1.0 O A:ALA461 3.9 15.6 1.0 OE2 A:GLU519 4.1 18.6 1.0 OE1 A:GLU319 4.2 28.1 1.0 CA A:SER462 4.4 17.6 1.0 OE2 A:GLU497 4.4 16.1 1.0 OE1 A:GLU497 4.4 16.2 1.0 OE1 A:GLU519 4.4 18.0 1.0 CD A:GLU519 4.6 18.1 1.0 NE2 A:HIS500 4.7 15.3 1.0 O A:HOH1699 4.7 27.4 1.0 NE2 A:HIS496 4.7 15.8 1.0 C A:ALA461 4.7 15.9 1.0 CZ A:TYR580 4.7 18.6 1.0 CD A:GLU319 4.8 27.7 1.0 CD A:GLU497 4.8 15.9 1.0 N A:GLU463 4.9 19.9 1.0 CD A:GLU463 5.0 23.4 1.0 N A:SER462 5.0 16.8 1.0 CB A:SER462 5.0 17.6 1.0

C.T.Webb, S.Mcgowan, W.Yang, N.Drinkwater. Conformational Dynamics of the Plasmodium Falciparum M1 Aminopeptidase. To Be Published.