Magnesium in PDB 9ixe: Crystal Structure of Copper-Bound N(Omega)-Hydroxy-L-Arginine Hydrolase Without Oxidized CYS86

Enzymatic activity of Crystal Structure of Copper-Bound N(Omega)-Hydroxy-L-Arginine Hydrolase Without Oxidized CYS86

All present enzymatic activity of Crystal Structure of Copper-Bound N(Omega)-Hydroxy-L-Arginine Hydrolase Without Oxidized CYS86:
3.5.3.25;

Protein crystallography data

The structure of Crystal Structure of Copper-Bound N(Omega)-Hydroxy-L-Arginine Hydrolase Without Oxidized CYS86, PDB code: 9ixe 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) 43.65 / 1.58
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 46.502, 46.981, 59.559, 83.57, 84.69, 70.09
R / Rfree (%) 17.9 / 21.7

Other elements in 9ixe:

The structure of Crystal Structure of Copper-Bound N(Omega)-Hydroxy-L-Arginine Hydrolase Without Oxidized CYS86 also contains other interesting chemical elements:

Manganese (Mn) 2 atoms
Copper (Cu) 3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Copper-Bound N(Omega)-Hydroxy-L-Arginine Hydrolase Without Oxidized CYS86 (pdb code 9ixe). 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 Copper-Bound N(Omega)-Hydroxy-L-Arginine Hydrolase Without Oxidized CYS86, PDB code: 9ixe:

Magnesium binding site 1 out of 1 in 9ixe

Go back to Magnesium Binding Sites List in 9ixe
Magnesium binding site 1 out of 1 in the Crystal Structure of Copper-Bound N(Omega)-Hydroxy-L-Arginine Hydrolase Without Oxidized CYS86


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 Copper-Bound N(Omega)-Hydroxy-L-Arginine Hydrolase Without Oxidized CYS86 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg403

b:24.7
occ:0.56
 O A:HOH653 2.0 31.7 1.0
O A:ASN77 2.0 22.7 1.0
O A:HOH584 2.0 28.5 1.0
O A:HOH729 2.2 30.2 1.0
O A:HOH655 2.2 28.4 1.0
O A:HOH538 2.3 24.9 1.0
C A:ASN77 3.0 23.1 1.0
O A:ILE235 3.8 16.6 1.0
N A:LEU78 3.8 20.9 1.0
N A:ASN77 3.9 25.9 1.0
CA A:LEU78 4.0 20.4 1.0
CA A:ASN77 4.0 27.9 1.0
C A:ASP76 4.1 24.2 1.0
O A:HOH710 4.1 31.1 1.0
O A:ASP76 4.2 30.5 1.0
O A:HOH511 4.3 32.6 1.0
O A:HOH714 4.3 37.2 1.0
O A:GLY75 4.4 27.0 1.0
N A:THR79 4.6 13.9 1.0
C A:LEU78 4.7 17.7 1.0
O A:SER72 4.7 24.2 1.0
OG1 A:THR79 4.7 19.1 1.0
C A:ILE235 4.8 14.0 1.0
CA A:ASP76 4.8 31.4 1.0
O A:LEU234 4.9 16.9 1.0
CA A:ILE235 4.9 15.6 1.0
O A:ILE73 5.0 27.8 1.0
O A:HOH547 5.0 25.3 1.0

Reference:

K.Oda, Y.Matoba. Copper Inactivates Dcsb By Oxidizing the Metal Ligand CYS86 to Sulfinic Acid. Febs J. 2024.
ISSN: ISSN 1742-464X
DOI: 10.1111/FEBS.17325
Page generated: Wed Nov 27 19:10:14 2024

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