Magnesium in PDB 9iq9: Crystal Structure of Copper-Bound N(Omega)-Hydroxy-L-Arginine Hydrolase with Reduced CYS86

Enzymatic activity of Crystal Structure of Copper-Bound N(Omega)-Hydroxy-L-Arginine Hydrolase with Reduced CYS86

All present enzymatic activity of Crystal Structure of Copper-Bound N(Omega)-Hydroxy-L-Arginine Hydrolase with Reduced CYS86:
3.5.3.25;

Protein crystallography data

The structure of Crystal Structure of Copper-Bound N(Omega)-Hydroxy-L-Arginine Hydrolase with Reduced CYS86, PDB code: 9iq9 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 9iq9:

The structure of Crystal Structure of Copper-Bound N(Omega)-Hydroxy-L-Arginine Hydrolase with Reduced 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 with Reduced CYS86 (pdb code 9iq9). 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 with Reduced CYS86, PDB code: 9iq9:

Magnesium binding site 1 out of 1 in 9iq9

Go back to Magnesium Binding Sites List in 9iq9
Magnesium binding site 1 out of 1 in the Crystal Structure of Copper-Bound N(Omega)-Hydroxy-L-Arginine Hydrolase with Reduced 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 with Reduced CYS86 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg403

b:33.8
occ:1.00
 O A:ASN77 2.0 22.8 1.0
O A:HOH652 2.0 31.9 1.0
O A:HOH579 2.0 28.2 1.0
O A:HOH543 2.3 24.7 1.0
O A:HOH670 2.3 28.4 1.0
O A:HOH730 2.3 29.9 1.0
C A:ASN77 3.0 23.7 1.0
N A:LEU78 3.8 21.1 1.0
N A:ASN77 3.8 26.1 1.0
O A:ILE235 3.8 16.4 1.0
CA A:LEU78 4.0 20.6 1.0
CA A:ASN77 4.0 28.0 1.0
C A:ASP76 4.0 24.1 1.0
O A:HOH713 4.1 31.3 1.0
O A:ASP76 4.2 30.6 1.0
O A:HOH717 4.3 37.1 1.0
O A:HOH512 4.3 32.6 1.0
O A:GLY75 4.4 27.1 1.0
N A:THR79 4.5 13.9 1.0
C A:LEU78 4.6 17.8 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 13.9 1.0
CA A:ASP76 4.8 31.7 1.0
O A:LEU234 4.9 17.1 1.0
CA A:ILE235 4.9 15.7 1.0
O A:ILE73 4.9 27.9 1.0
O A:HOH552 5.0 25.2 1.0

Reference:

K.Oda, K.Komaguchi, Y.Matoba. Copper Inactivates Dcsb By Oxidation of the CYS86 to Cysteine Sulfinic Aicd To Be Published.
Page generated: Sat Oct 5 09:36:54 2024

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