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Magnesium in PDB 8iuv: Crystal Structure of Manganese-Free N(Omega)-Hydroxy-L-Arginine Hydrolase with Oxidized CYS86

Enzymatic activity of Crystal Structure of Manganese-Free N(Omega)-Hydroxy-L-Arginine Hydrolase with Oxidized CYS86

All present enzymatic activity of Crystal Structure of Manganese-Free N(Omega)-Hydroxy-L-Arginine Hydrolase with Oxidized CYS86:
3.5.3.25;

Protein crystallography data

The structure of Crystal Structure of Manganese-Free N(Omega)-Hydroxy-L-Arginine Hydrolase with Oxidized CYS86, PDB code: 8iuv 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) 43.92 / 1.75
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 45.876, 46.683, 58.222, 85.39, 86.78, 70.54
R / Rfree (%) 15.8 / 20.1

Other elements in 8iuv:

The structure of Crystal Structure of Manganese-Free N(Omega)-Hydroxy-L-Arginine Hydrolase with Oxidized CYS86 also contains other interesting chemical elements:

Manganese (Mn) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Manganese-Free N(Omega)-Hydroxy-L-Arginine Hydrolase with Oxidized CYS86 (pdb code 8iuv). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of Manganese-Free N(Omega)-Hydroxy-L-Arginine Hydrolase with Oxidized CYS86, PDB code: 8iuv:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 8iuv

Go back to Magnesium Binding Sites List in 8iuv
Magnesium binding site 1 out of 4 in the Crystal Structure of Manganese-Free N(Omega)-Hydroxy-L-Arginine Hydrolase with 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 Manganese-Free N(Omega)-Hydroxy-L-Arginine Hydrolase with Oxidized CYS86 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:8.4
occ:1.00
 OD1 A:ASP109 2.1 9.0 1.0
OD2 A:ASP200 2.1 12.4 1.0
O A:HOH550 2.1 10.8 1.0
OD2 A:ASP198 2.2 12.5 1.0
ND1 A:HIS111 2.3 10.3 1.0
OD1 A:ASP200 2.3 10.1 1.0
CG A:ASP200 2.5 14.1 1.0
CG A:ASP109 3.0 9.7 1.0
CG A:ASP198 3.1 10.4 1.0
CE1 A:HIS111 3.1 12.7 1.0
CG A:HIS111 3.3 10.3 1.0
MN A:MN401 3.3 12.1 1.0
OD2 A:ASP109 3.4 8.6 1.0
OD1 A:ASP198 3.7 9.7 1.0
CB A:HIS111 3.7 11.1 1.0
N A:HIS111 3.8 10.1 1.0
O A:HOH505 4.0 19.2 1.0
N A:GLY110 4.0 9.1 1.0
CB A:ASP200 4.0 12.5 1.0
CB A:ASP198 4.0 10.9 1.0
O A:HOH692 4.3 27.3 1.0
NE2 A:HIS111 4.3 12.8 1.0
O A:HOH604 4.3 13.6 1.0
CB A:ASP109 4.4 7.8 1.0
CA A:HIS111 4.4 10.3 1.0
OD1 A:ASP113 4.4 10.6 1.0
CD2 A:HIS111 4.4 13.7 1.0
O A:HOH598 4.4 22.8 1.0
CA A:GLY110 4.6 9.3 1.0
C A:GLY110 4.6 11.9 1.0
CA A:ASP109 4.7 9.0 1.0
C A:ASP109 4.7 10.7 1.0
OD2 A:ASP113 4.8 11.6 1.0
CA A:ASP200 5.0 9.0 1.0
CG A:ASP113 5.0 12.6 1.0

Magnesium binding site 2 out of 4 in 8iuv

Go back to Magnesium Binding Sites List in 8iuv
Magnesium binding site 2 out of 4 in the Crystal Structure of Manganese-Free N(Omega)-Hydroxy-L-Arginine Hydrolase with Oxidized CYS86


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 Manganese-Free N(Omega)-Hydroxy-L-Arginine Hydrolase with Oxidized CYS86 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg401

b:18.5
occ:1.00
 O B:HOH590 2.0 22.4 1.0
OE2 B:GLU241 2.1 20.4 1.0
O B:HOH503 2.1 18.4 1.0
OD2 B:ASP200 2.1 18.5 1.0
OD2 B:ASP198 2.2 16.7 1.0
OD1 B:ASP198 2.3 14.5 1.0
CG B:ASP198 2.6 15.4 1.0
CG B:ASP200 3.0 18.2 1.0
CD B:GLU241 3.2 20.9 1.0
O B:HOH569 3.5 18.2 1.0
CB B:ASP200 3.7 18.4 1.0
O B:HOH630 3.8 18.4 1.0
O B:HOH572 3.8 30.1 1.0
MG B:MG403 3.9 11.3 1.0
OD1 B:ASP200 3.9 15.6 1.0
CG B:GLU241 4.0 16.6 1.0
OE1 B:GLU241 4.1 19.9 1.0
CB B:GLU241 4.1 16.1 1.0
CB B:ASP198 4.1 14.1 1.0
O B:ASP210 4.1 30.6 1.0
OD1 B:ASP210 4.4 40.5 1.0
N B:ASP200 4.5 12.8 1.0
CA B:ASP200 4.7 15.5 1.0
SG B:CSO86 4.8 16.8 0.5
OD B:CSO86 4.9 17.7 0.5
O B:HOH703 4.9 33.0 1.0
SG B:CSO86 4.9 16.6 0.5
OD2 B:ASP109 5.0 14.1 1.0

Magnesium binding site 3 out of 4 in 8iuv

Go back to Magnesium Binding Sites List in 8iuv
Magnesium binding site 3 out of 4 in the Crystal Structure of Manganese-Free N(Omega)-Hydroxy-L-Arginine Hydrolase with Oxidized CYS86


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Manganese-Free N(Omega)-Hydroxy-L-Arginine Hydrolase with Oxidized CYS86 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg402

b:29.7
occ:1.00
 O B:HOH622 1.9 25.0 1.0
O B:HOH671 2.1 23.7 1.0
O B:HOH537 2.1 28.0 1.0
OE2 B:GLU162 2.1 24.2 1.0
O B:HOH670 2.2 29.7 1.0
O B:HOH539 2.2 30.6 1.0
CD B:GLU162 3.2 23.4 1.0
OE1 B:GLU162 3.5 24.1 1.0
OD1 B:ASP159 3.8 43.3 1.0
ND2 B:ASN115 4.1 21.0 1.0
O B:HIS111 4.1 24.6 1.0
O B:HOH518 4.3 27.1 1.0
CB B:HIS111 4.4 16.4 1.0
ND1 B:HIS111 4.4 24.9 1.0
CG B:GLU162 4.5 22.3 1.0
N B:ASP159 4.6 26.4 1.0
O B:HOH521 4.7 31.3 1.0
C B:HIS111 4.8 23.2 1.0
CB B:GLU162 4.8 25.4 1.0
CG B:ASP159 4.9 40.4 1.0
O B:HOH674 4.9 23.3 1.0
CG B:HIS111 4.9 20.2 1.0
CA B:HIS111 4.9 15.1 1.0
CG2 B:ILE158 4.9 25.3 1.0
CA B:ILE158 5.0 22.8 1.0
CG B:ASN115 5.0 23.1 1.0

Magnesium binding site 4 out of 4 in 8iuv

Go back to Magnesium Binding Sites List in 8iuv
Magnesium binding site 4 out of 4 in the Crystal Structure of Manganese-Free N(Omega)-Hydroxy-L-Arginine Hydrolase with Oxidized CYS86


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of Manganese-Free N(Omega)-Hydroxy-L-Arginine Hydrolase with Oxidized CYS86 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg403

b:11.3
occ:1.00
 OD B:CSO86 1.9 17.7 0.5
OD2 B:ASP113 2.1 15.2 1.0
OD2 B:ASP109 2.1 14.1 1.0
O B:HOH630 2.1 18.4 1.0
OD2 B:ASP198 2.1 16.7 1.0
O B:HOH569 2.1 18.2 1.0
SG B:CSO86 2.6 16.8 0.5
CG B:ASP113 3.1 15.1 1.0
SG B:CSO86 3.1 16.6 0.5
CG B:ASP109 3.1 17.0 1.0
CG B:ASP198 3.2 15.4 1.0
OD1 B:ASP113 3.4 15.9 1.0
OD1 B:ASP109 3.5 20.2 1.0
CB B:ASP198 3.5 14.1 1.0
CB B:CSO86 3.7 15.9 0.5
CB B:CSO86 3.8 15.8 0.5
MG B:MG401 3.9 18.5 1.0
O B:HOH590 3.9 22.4 1.0
OH B:TYR107 4.0 15.3 1.0
OD2 B:ASP200 4.2 18.5 1.0
O B:GLY126 4.2 20.1 1.0
OD1 B:ASP198 4.3 14.5 1.0
CB B:ASP113 4.4 12.1 1.0
CB B:ASP109 4.4 14.8 1.0
CE1 B:TYR107 4.4 12.6 1.0
OE2 B:GLU241 4.5 20.4 1.0
CZ B:TYR107 4.7 15.8 1.0
CD B:GLU241 4.7 20.9 1.0
OE1 B:GLU241 4.8 19.9 1.0
OD1 B:ASP200 4.8 15.6 1.0
CG B:ASP200 4.9 18.2 1.0
NE2 B:HIS196 5.0 19.9 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: Fri Oct 4 11:01:25 2024

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