Magnesium in PDB 3vat: Crystal Structure of Dnpep, Znmg Form

All present enzymatic activity of Crystal Structure of Dnpep, Znmg Form:
3.4.11.21;

The structure of Crystal Structure of Dnpep, Znmg Form, PDB code: 3vat was solved by P.D.Kiser, Y.Chen, K.Palczewski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	73.65 / 2.10
Space group	F 4 3 2
Cell size a, b, c (Å), α, β, γ (°)	244.269, 244.269, 244.269, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 21.1

The structure of Crystal Structure of Dnpep, Znmg Form also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Magnesium atom in the Crystal Structure of Dnpep, Znmg Form (pdb code 3vat). 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 Dnpep, Znmg Form, PDB code: 3vat:

Magnesium binding site 1 out of 1 in the Crystal Structure of Dnpep, Znmg Form


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 Dnpep, Znmg Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg502 b:9.1 occ:1.00 OD1 A:ASP285 1.9 15.4 1.0 O A:HOH698 2.0 18.9 1.0 OD1 A:ASP367 2.1 16.2 1.0 NE2 A:HIS115 2.1 17.2 1.0 O A:HOH609 2.1 26.8 1.0 OD2 A:ASP367 2.2 17.3 1.0 CG A:ASP367 2.5 16.7 1.0 CG A:ASP285 2.9 16.0 1.0 CE1 A:HIS115 3.0 17.2 1.0 CD2 A:HIS115 3.2 15.2 1.0 OD2 A:ASP285 3.4 16.9 1.0 ZN A:ZN501 3.4 23.0 1.0 O A:HOH608 3.9 23.9 1.0 OE1 A:GLU322 3.9 18.5 1.0 OE2 A:GLU323 4.0 17.1 1.0 CB A:ASN286 4.0 16.0 1.0 CB A:ASP367 4.1 17.3 1.0 CD A:GLU322 4.2 19.2 1.0 ND1 A:HIS115 4.3 17.2 1.0 CB A:ASP285 4.3 16.6 1.0 O A:HOH713 4.3 13.8 0.5 OE2 A:GLU322 4.3 22.3 1.0 CG A:ASN286 4.3 15.6 1.0 CG A:HIS115 4.3 15.4 1.0 ND2 A:ASN286 4.6 15.4 1.0 O A:HOH710 4.7 35.3 1.0 N A:MET368 4.7 15.7 1.0 CD A:GLU323 4.8 16.1 1.0 CA A:ASP285 4.8 17.1 1.0 CA A:ASP367 4.9 16.7 1.0 OD1 A:ASN286 4.9 17.2 1.0 C A:ASP285 4.9 18.6 1.0 CA A:ASN286 5.0 15.7 1.0 OE1 A:GLU323 5.0 17.7 1.0

Y.Chen, E.R.Farquhar, M.R.Chance, K.Palczewski, P.D.Kiser. Insights Into Substrate Specificity and Metal Activation of Mammalian Tetrahedral Aspartyl Aminopeptidase. J.Biol.Chem. V. 287 13356 2012.
ISSN: ISSN 0021-9258
PubMed: 22356908
DOI: 10.1074/JBC.M112.347518