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:
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
|