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Manganese in PDB 7euk: Crystal Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase in Complex with L-Orn

Enzymatic activity of Crystal Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase in Complex with L-Orn

All present enzymatic activity of Crystal Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase in Complex with L-Orn:
3.5.3.25;

Protein crystallography data

The structure of Crystal Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase in Complex with L-Orn, PDB code: 7euk 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) 44.00 / 1.40
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 46.392, 46.963, 59.317, 83.53, 84.71, 70.14
R / Rfree (%) 15.8 / 17.9

Other elements in 7euk:

The structure of Crystal Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase in Complex with L-Orn also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase in Complex with L-Orn (pdb code 7euk). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Crystal Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase in Complex with L-Orn, PDB code: 7euk:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 7euk

Go back to Manganese Binding Sites List in 7euk
Manganese binding site 1 out of 4 in the Crystal Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase in Complex with L-Orn


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase in Complex with L-Orn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn401

b:7.1
occ:1.00
OD2 A:ASP109 2.1 5.9 1.0
O A:HOH621 2.2 9.3 1.0
OD2 A:ASP113 2.2 7.1 1.0
OD2 A:ASP198 2.3 6.0 1.0
O A:HOH522 2.4 7.9 1.0
SG A:CYS86 2.5 8.0 1.0
CG A:ASP113 3.2 8.2 1.0
CG A:ASP109 3.2 5.7 1.0
CG A:ASP198 3.2 6.6 1.0
MN A:MN402 3.4 7.0 1.0
CB A:CYS86 3.4 7.2 1.0
OD1 A:ASP113 3.4 7.7 1.0
CB A:ASP198 3.5 6.0 1.0
OD1 A:ASP109 3.5 6.4 1.0
OH A:TYR107 4.0 7.6 1.0
OE2 A:GLU241 4.2 10.4 1.0
O A:GLY126 4.3 14.8 1.0
OD1 A:ASP198 4.3 6.8 1.0
CD A:GLU241 4.4 10.6 1.0
CE1 A:TYR107 4.5 6.8 1.0
CB A:ASP109 4.5 6.3 1.0
CB A:ASP113 4.5 8.9 1.0
OE1 A:GLU241 4.6 10.8 1.0
CZ A:TYR107 4.7 6.7 1.0
CA A:CYS86 4.8 7.6 1.0
NE2 A:HIS196 4.9 8.8 1.0
OD2 A:ASP200 4.9 8.0 1.0
O A:HOH507 4.9 11.7 1.0
CA A:ASP198 4.9 6.1 1.0

Manganese binding site 2 out of 4 in 7euk

Go back to Manganese Binding Sites List in 7euk
Manganese binding site 2 out of 4 in the Crystal Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase in Complex with L-Orn


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase in Complex with L-Orn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn402

b:7.0
occ:1.00
OD1 A:ASP109 2.1 6.4 1.0
OD2 A:ASP200 2.2 8.0 1.0
OD2 A:ASP198 2.2 6.0 1.0
O A:HOH522 2.2 7.9 1.0
ND1 A:HIS111 2.3 7.6 1.0
OD1 A:ASP200 2.4 7.5 1.0
CG A:ASP200 2.6 7.0 1.0
CG A:ASP198 3.1 6.6 1.0
CG A:ASP109 3.1 5.7 1.0
CE1 A:HIS111 3.1 7.8 1.0
CG A:HIS111 3.3 6.5 1.0
MN A:MN401 3.4 7.1 1.0
OD2 A:ASP109 3.4 5.9 1.0
OD1 A:ASP198 3.6 6.8 1.0
CB A:HIS111 3.6 6.4 1.0
N A:HIS111 3.8 6.8 1.0
O A:HOH507 3.8 11.7 1.0
CB A:ASP198 4.1 6.0 1.0
N A:GLY110 4.1 6.5 1.0
CB A:ASP200 4.1 7.0 1.0
NE2 A:HIS111 4.3 7.7 1.0
OD1 A:ASP113 4.4 7.7 1.0
CA A:HIS111 4.4 7.3 1.0
O A:HOH615 4.4 17.4 1.0
CD2 A:HIS111 4.4 7.7 1.0
O A:HOH621 4.4 9.3 1.0
CB A:ASP109 4.4 6.3 1.0
C A:GLY110 4.6 6.4 1.0
O A:HOH788 4.7 25.7 1.0
CA A:GLY110 4.7 7.7 1.0
CA A:ASP109 4.8 6.8 1.0
C A:ASP109 4.8 7.7 1.0
OD2 A:ASP113 4.8 7.1 1.0
CG A:ASP113 5.0 8.2 1.0

Manganese binding site 3 out of 4 in 7euk

Go back to Manganese Binding Sites List in 7euk
Manganese binding site 3 out of 4 in the Crystal Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase in Complex with L-Orn


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase in Complex with L-Orn within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn401

b:8.5
occ:1.00
OD2 B:ASP109 2.2 8.0 1.0
O B:HOH627 2.2 12.4 1.0
OD2 B:ASP113 2.2 7.8 1.0
OD2 B:ASP198 2.3 8.5 1.0
O B:HOH501 2.3 10.2 1.0
SG B:CYS86 2.5 8.8 1.0
CG B:ASP113 3.1 8.2 1.0
CG B:ASP109 3.2 7.8 1.0
CG B:ASP198 3.2 8.2 1.0
MN B:MN402 3.3 9.9 1.0
OD1 B:ASP113 3.4 9.3 1.0
CB B:CYS86 3.4 9.3 1.0
OD1 B:ASP109 3.5 8.1 1.0
CB B:ASP198 3.5 8.0 1.0
NE B:ORN403 3.9 21.7 1.0
OH B:TYR107 4.1 8.3 1.0
OE2 B:GLU241 4.3 11.1 1.0
OD1 B:ASP198 4.3 8.8 1.0
O B:GLY126 4.4 16.0 1.0
CE1 B:TYR107 4.5 8.0 1.0
CD B:GLU241 4.5 10.2 1.0
CB B:ASP109 4.5 8.5 1.0
CB B:ASP113 4.5 8.5 1.0
CZ B:TYR107 4.7 8.5 1.0
OE1 B:GLU241 4.8 11.8 1.0
CA B:CYS86 4.8 8.8 1.0
NE2 B:HIS196 4.9 9.7 1.0
OD2 B:ASP200 4.9 9.6 1.0
CA B:ASP198 5.0 8.0 1.0

Manganese binding site 4 out of 4 in 7euk

Go back to Manganese Binding Sites List in 7euk
Manganese binding site 4 out of 4 in the Crystal Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase in Complex with L-Orn


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase in Complex with L-Orn within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn402

b:9.9
occ:1.00
OD1 B:ASP109 2.1 8.1 1.0
OD2 B:ASP200 2.1 9.6 1.0
O B:HOH501 2.2 10.2 1.0
ND1 B:HIS111 2.2 9.3 1.0
OD2 B:ASP198 2.3 8.5 1.0
OD1 B:ASP200 2.4 9.2 1.0
CG B:ASP200 2.6 10.2 1.0
CG B:ASP109 3.1 7.8 1.0
CE1 B:HIS111 3.1 9.7 1.0
CG B:ASP198 3.1 8.2 1.0
CG B:HIS111 3.3 9.5 1.0
MN B:MN401 3.3 8.5 1.0
OD2 B:ASP109 3.4 8.0 1.0
OD1 B:ASP198 3.6 8.8 1.0
NE B:ORN403 3.7 21.7 1.0
CB B:HIS111 3.7 9.2 1.0
N B:HIS111 3.9 9.2 1.0
N B:GLY110 4.1 8.6 1.0
CB B:ASP200 4.1 9.6 1.0
CB B:ASP198 4.1 8.0 1.0
O B:HOH627 4.2 12.4 1.0
NE2 B:HIS111 4.3 12.7 1.0
OD1 B:ASP113 4.3 9.3 1.0
CD2 B:HIS111 4.4 11.5 1.0
CB B:ASP109 4.4 8.5 1.0
CA B:HIS111 4.5 9.5 1.0
O B:HOH584 4.5 10.4 1.0
C B:GLY110 4.6 9.2 1.0
CA B:GLY110 4.7 8.2 1.0
CD B:ORN403 4.7 23.8 1.0
CA B:ASP109 4.8 9.0 1.0
OD2 B:ASP113 4.8 7.8 1.0
C B:ASP109 4.8 8.1 1.0
CG B:ASP113 5.0 8.2 1.0

Reference:

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
Page generated: Sun Oct 6 08:33:41 2024

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