Magnesium in PDB 1e33: Crystal Structure of An Arylsulfatase A Mutant P426L

All present enzymatic activity of Crystal Structure of An Arylsulfatase A Mutant P426L:
3.1.6.8;

The structure of Crystal Structure of An Arylsulfatase A Mutant P426L, PDB code: 1e33 was solved by R.Von Buelow, B.Schmidt, T.Dierks, K.Von Figura, I.Uson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.50
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	131.400, 131.400, 192.000, 90.00, 90.00, 90.00
R / Rfree (%)	18.5 / 25

The binding sites of Magnesium atom in the Crystal Structure of An Arylsulfatase A Mutant P426L (pdb code 1e33). 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 An Arylsulfatase A Mutant P426L, PDB code: 1e33:

Magnesium binding site 1 out of 1 in the Crystal Structure of An Arylsulfatase A Mutant P426L


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 An Arylsulfatase A Mutant P426L within 5.0Å range: probe atom residue distance (Å) B Occ P:Mg603 b:24.0 occ:1.00 OD2 P:ASP281 2.3 24.8 1.0 OD1 P:ASP29 2.3 46.0 1.0 OG1 P:DDZ69 2.4 28.5 1.0 OD1 P:ASP30 2.4 22.3 1.0 OD1 P:ASN282 2.6 31.4 1.0 OD1 P:ASP281 2.7 28.4 1.0 CG P:ASP281 2.8 24.5 1.0 CB P:DDZ69 3.5 32.0 1.0 CG P:ASN282 3.5 30.2 1.0 CG P:ASP29 3.5 31.1 1.0 CG P:ASP30 3.5 19.3 1.0 ND2 P:ASN282 3.6 21.2 1.0 N P:ASP30 3.7 19.8 1.0 CA P:DDZ69 3.8 28.8 1.0 N P:DDZ69 4.0 31.4 1.0 OD2 P:ASP29 4.0 28.9 1.0 OG2 P:DDZ69 4.1 33.3 1.0 NH2 P:ARG73 4.2 26.3 1.0 CB P:ASP281 4.3 23.8 1.0 OD2 P:ASP30 4.3 18.5 1.0 CA P:ASP30 4.4 21.9 1.0 O P:HOH2024 4.4 30.2 1.0 C P:ASP29 4.4 23.3 1.0 CB P:ASP30 4.5 16.9 1.0 CA P:ASP29 4.5 23.5 1.0 NZ P:LYS123 4.5 34.3 1.0 CD2 P:HIS229 4.5 17.6 1.0 CB P:ASP29 4.6 19.0 1.0 NZ P:LYS302 4.6 20.8 1.0 CE P:LYS302 4.8 28.6 1.0 C P:LEU68 4.8 31.3 1.0 CB P:ASN282 4.8 24.1 1.0 N P:ASN282 5.0 20.6 1.0

R.Von Bulow, B.Schmidt, T.Dierks, N.Schwabauer, K.Schilling, E.Weber, I.Uson, K.Von Figura. Defective Oligomerization of Arylsulfatase A As A Cause of Its Instability in Lysosomes and Metachromatic Leukodystrophy. J. Biol. Chem. V. 277 9455 2002.
ISSN: ISSN 0021-9258
PubMed: 11777924
DOI: 10.1074/JBC.M111993200