Magnesium in PDB 7eul: Crystal Structure of C86H-H196S Mutant of N(Omega)-Hydroxy-L-Arginine Hydrolase

All present enzymatic activity of Crystal Structure of C86H-H196S Mutant of N(Omega)-Hydroxy-L-Arginine Hydrolase:
3.5.3.25;

The structure of Crystal Structure of C86H-H196S Mutant of N(Omega)-Hydroxy-L-Arginine Hydrolase, PDB code: 7eul was solved by K.Oda, Y.Matoba, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.93 / 1.45
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.499, 50.343, 52.941, 90, 99.42, 90
R / Rfree (%)	16.9 / 19.3

The structure of Crystal Structure of C86H-H196S Mutant of N(Omega)-Hydroxy-L-Arginine Hydrolase also contains other interesting chemical elements:

Manganese

(Mn)

3 atoms

The binding sites of Magnesium atom in the Crystal Structure of C86H-H196S Mutant of N(Omega)-Hydroxy-L-Arginine Hydrolase (pdb code 7eul). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of C86H-H196S Mutant of N(Omega)-Hydroxy-L-Arginine Hydrolase, PDB code: 7eul:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of C86H-H196S Mutant of N(Omega)-Hydroxy-L-Arginine Hydrolase


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 C86H-H196S Mutant of N(Omega)-Hydroxy-L-Arginine Hydrolase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg404 b:18.9 occ:1.00 O A:HOH518 2.1 20.0 1.0 O A:HOH683 2.1 24.1 1.0 O A:HOH706 2.1 24.3 1.0 OE1 A:GLU99 4.2 20.4 1.0 NZ A:LYS74 4.2 25.4 1.0 O A:HOH583 4.2 18.9 1.0 O A:HOH712 4.7 38.4 1.0 OE2 A:GLU99 4.7 24.6 1.0 CD A:GLU99 4.8 19.1 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of C86H-H196S Mutant of N(Omega)-Hydroxy-L-Arginine Hydrolase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of C86H-H196S Mutant of N(Omega)-Hydroxy-L-Arginine Hydrolase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg405 b:27.5 occ:1.00 O A:HOH733 1.9 27.5 1.0 O A:HOH579 2.1 35.9 1.0 O A:HOH684 2.1 33.2 1.0 O A:HOH670 2.2 27.3 1.0 O A:HOH731 2.2 39.0 1.0 O A:HOH516 2.4 32.3 1.0 O A:HOH745 3.4 37.9 1.0 O A:HOH607 4.0 19.1 1.0 O A:ASP76 4.1 27.8 1.0 O A:HOH718 4.1 32.4 1.0 O A:HOH526 4.2 24.8 1.0 O A:ASN77 4.3 24.0 1.0 C A:ASP76 4.4 22.9 1.0 O A:HOH543 4.4 23.9 1.0 O A:GLY75 4.5 20.1 1.0 CA A:ASP76 4.5 19.8 1.0 O A:LEU234 4.6 21.4 1.0 OD1 A:ASP76 4.7 42.4 1.0 O A:ILE235 4.8 16.5 1.0 CA A:ILE235 4.9 16.1 1.0 C A:ASN77 5.0 19.9 1.0

K.Oda, T.Sakaguchi, Y.Matoba. Catalytic Mechanism of Dcsb: Arginase Framework Used For Hydrolyzing Its Inhibitor. Protein Sci. V. 31 E4338 2022.
ISSN: ESSN 1469-896X
PubMed: 35634777
DOI: 10.1002/PRO.4338