Magnesium in PDB 1auk: Human Arylsulfatase A

All present enzymatic activity of Human Arylsulfatase A:
3.1.6.8;

The structure of Human Arylsulfatase A, PDB code: 1auk was solved by G.Lukatela, N.Krauss, K.Theis, V.Gieselmann, K.Von Figura, W.Saenger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.10
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	132.630, 132.630, 192.060, 90.00, 90.00, 90.00
R / Rfree (%)	23.2 / 27.3

The binding sites of Magnesium atom in the Human Arylsulfatase A (pdb code 1auk). 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 Human Arylsulfatase A, PDB code: 1auk:

Magnesium binding site 1 out of 1 in the Human Arylsulfatase A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human Arylsulfatase A within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg603 b:24.2 occ:1.00 OD2 A:ASP281 2.2 31.7 1.0 OD1 A:ASP30 2.2 19.8 1.0 OD1 A:ASP29 2.3 33.9 1.0 OD1 A:ASN282 2.6 29.4 1.0 OD1 A:ASP281 2.6 35.8 1.0 CG A:ASP281 2.8 33.0 1.0 CG A:ASN282 3.4 31.0 1.0 CG A:ASP30 3.4 18.7 1.0 ND2 A:ASN282 3.5 26.4 1.0 N A:ASP30 3.5 27.3 1.0 CG A:ASP29 3.5 34.8 1.0 CA A:FGL69 4.0 35.7 1.0 OD2 A:ASP30 4.2 23.7 1.0 N A:FGL69 4.2 30.3 1.0 C A:ASP29 4.3 24.4 1.0 CA A:ASP30 4.3 26.4 1.0 CB A:ASP281 4.3 28.6 1.0 OD2 A:ASP29 4.3 31.6 1.0 CA A:ASP29 4.3 29.6 1.0 CB A:ASP30 4.3 21.2 1.0 NZ A:LYS123 4.4 33.1 1.0 CD2 A:HIS229 4.4 28.3 1.0 CB A:ASP29 4.5 28.1 1.0 NH2 A:ARG73 4.5 35.3 1.0 NZ A:LYS302 4.6 31.7 1.0 CB A:ASN282 4.7 28.4 1.0 CE A:LYS302 4.8 32.5 1.0 N A:ASN282 4.9 25.1 1.0 C A:LEU68 5.0 30.4 1.0

G.Lukatela, N.Krauss, K.Theis, T.Selmer, V.Gieselmann, K.Von Figura, W.Saenger. Crystal Structure of Human Arylsulfatase A: the Aldehyde Function and the Metal Ion at the Active Site Suggest A Novel Mechanism For Sulfate Ester Hydrolysis. Biochemistry V. 37 3654 1998.
ISSN: ISSN 0006-2960
PubMed: 9521684
DOI: 10.1021/BI9714924