Manganese in PDB 6luh: High Resolution Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase
Enzymatic activity of High Resolution Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase
All present enzymatic activity of High Resolution Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase:
3.5.3.25;
Protein crystallography data
The structure of High Resolution Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase, PDB code: 6luh
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)
|
44.09 /
1.50
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
46.326,
47.057,
59.261,
83.57,
84.63,
70.13
|
R / Rfree (%)
|
20 /
23
|
Other elements in 6luh:
The structure of High Resolution Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase also contains other interesting chemical elements:
Manganese Binding Sites:
The binding sites of Manganese atom in the High Resolution Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase
(pdb code 6luh). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the
High Resolution Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase, PDB code: 6luh:
Jump to Manganese binding site number:
1;
2;
3;
4;
Manganese binding site 1 out
of 4 in 6luh
Go back to
Manganese Binding Sites List in 6luh
Manganese binding site 1 out
of 4 in the High Resolution Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of High Resolution Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn401
b:5.7
occ:1.00
|
OD2
|
A:ASP109
|
2.2
|
5.2
|
1.0
|
OD2
|
A:ASP198
|
2.2
|
5.5
|
1.0
|
O
|
A:HOH623
|
2.2
|
8.0
|
1.0
|
OD2
|
A:ASP113
|
2.3
|
7.6
|
1.0
|
O
|
A:HOH549
|
2.4
|
5.8
|
1.0
|
SG
|
A:CYS86
|
2.5
|
6.2
|
1.0
|
CG
|
A:ASP198
|
3.2
|
6.9
|
1.0
|
CG
|
A:ASP113
|
3.2
|
5.8
|
1.0
|
CG
|
A:ASP109
|
3.2
|
4.1
|
1.0
|
CB
|
A:CYS86
|
3.4
|
4.4
|
1.0
|
OD1
|
A:ASP113
|
3.4
|
6.9
|
1.0
|
MN
|
A:MN402
|
3.4
|
5.7
|
1.0
|
CB
|
A:ASP198
|
3.5
|
6.8
|
1.0
|
OD1
|
A:ASP109
|
3.5
|
2.8
|
1.0
|
O
|
A:HOH503
|
3.9
|
18.5
|
1.0
|
OH
|
A:TYR107
|
4.0
|
5.6
|
1.0
|
OE2
|
A:GLU241
|
4.2
|
7.3
|
1.0
|
OD1
|
A:ASP198
|
4.3
|
7.2
|
1.0
|
O
|
A:GLY126
|
4.3
|
10.1
|
1.0
|
CD
|
A:GLU241
|
4.4
|
6.7
|
1.0
|
CE1
|
A:TYR107
|
4.4
|
5.1
|
1.0
|
CB
|
A:ASP109
|
4.5
|
4.4
|
1.0
|
CB
|
A:ASP113
|
4.5
|
4.5
|
1.0
|
OE1
|
A:GLU241
|
4.6
|
8.8
|
1.0
|
CZ
|
A:TYR107
|
4.7
|
3.3
|
1.0
|
CA
|
A:CYS86
|
4.8
|
5.0
|
1.0
|
NE2
|
A:HIS196
|
4.9
|
5.8
|
1.0
|
CA
|
A:ASP198
|
4.9
|
6.8
|
1.0
|
O
|
B:HOH732
|
4.9
|
16.9
|
1.0
|
OD2
|
A:ASP200
|
5.0
|
4.8
|
1.0
|
|
Manganese binding site 2 out
of 4 in 6luh
Go back to
Manganese Binding Sites List in 6luh
Manganese binding site 2 out
of 4 in the High Resolution Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of High Resolution Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn402
b:5.7
occ:1.00
|
OD1
|
A:ASP109
|
2.0
|
2.8
|
1.0
|
O
|
A:HOH549
|
2.1
|
5.8
|
1.0
|
OD2
|
A:ASP198
|
2.2
|
5.5
|
1.0
|
OD2
|
A:ASP200
|
2.2
|
4.8
|
1.0
|
ND1
|
A:HIS111
|
2.3
|
8.2
|
1.0
|
OD1
|
A:ASP200
|
2.4
|
3.9
|
1.0
|
CG
|
A:ASP200
|
2.6
|
5.0
|
1.0
|
CG
|
A:ASP109
|
3.0
|
4.1
|
1.0
|
CG
|
A:ASP198
|
3.0
|
6.9
|
1.0
|
CE1
|
A:HIS111
|
3.2
|
6.7
|
1.0
|
CG
|
A:HIS111
|
3.3
|
7.4
|
1.0
|
OD2
|
A:ASP109
|
3.4
|
5.2
|
1.0
|
MN
|
A:MN401
|
3.4
|
5.7
|
1.0
|
OD1
|
A:ASP198
|
3.6
|
7.2
|
1.0
|
CB
|
A:HIS111
|
3.6
|
6.8
|
1.0
|
N
|
A:HIS111
|
3.7
|
7.2
|
1.0
|
CB
|
A:ASP198
|
4.1
|
6.8
|
1.0
|
CB
|
A:ASP200
|
4.2
|
6.7
|
1.0
|
N
|
A:GLY110
|
4.2
|
5.2
|
1.0
|
CA
|
A:HIS111
|
4.3
|
7.1
|
1.0
|
O
|
A:HOH595
|
4.3
|
15.8
|
1.0
|
OD1
|
A:ASP113
|
4.3
|
6.9
|
1.0
|
NE2
|
A:HIS111
|
4.3
|
4.2
|
1.0
|
O
|
A:HOH525
|
4.4
|
13.5
|
1.0
|
O
|
A:HOH623
|
4.4
|
8.0
|
1.0
|
CB
|
A:ASP109
|
4.4
|
4.4
|
1.0
|
CD2
|
A:HIS111
|
4.4
|
7.2
|
1.0
|
O
|
B:HOH732
|
4.5
|
16.9
|
1.0
|
C
|
A:GLY110
|
4.6
|
7.1
|
1.0
|
O
|
A:HOH503
|
4.7
|
18.5
|
1.0
|
CA
|
A:GLY110
|
4.7
|
6.0
|
1.0
|
CA
|
A:ASP109
|
4.8
|
4.1
|
1.0
|
C
|
A:ASP109
|
4.8
|
4.6
|
1.0
|
OD2
|
A:ASP113
|
4.8
|
7.6
|
1.0
|
CG
|
A:ASP113
|
5.0
|
5.8
|
1.0
|
|
Manganese binding site 3 out
of 4 in 6luh
Go back to
Manganese Binding Sites List in 6luh
Manganese binding site 3 out
of 4 in the High Resolution Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 3 of High Resolution Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn401
b:6.7
occ:1.00
|
OD2
|
B:ASP113
|
2.1
|
4.0
|
1.0
|
OD2
|
B:ASP109
|
2.2
|
7.1
|
1.0
|
O
|
B:HOH588
|
2.2
|
7.5
|
1.0
|
O
|
B:HOH521
|
2.2
|
6.2
|
1.0
|
OD2
|
B:ASP198
|
2.3
|
7.5
|
1.0
|
SG
|
B:CYS86
|
2.5
|
7.4
|
1.0
|
O
|
B:HOH501
|
3.1
|
18.2
|
1.0
|
CG
|
B:ASP113
|
3.1
|
5.6
|
1.0
|
CG
|
B:ASP109
|
3.2
|
4.8
|
1.0
|
CG
|
B:ASP198
|
3.3
|
8.2
|
1.0
|
CB
|
B:CYS86
|
3.3
|
9.4
|
1.0
|
OD1
|
B:ASP113
|
3.3
|
6.9
|
1.0
|
MN
|
B:MN402
|
3.4
|
7.5
|
1.0
|
CB
|
B:ASP198
|
3.5
|
7.8
|
1.0
|
OD1
|
B:ASP109
|
3.6
|
5.7
|
1.0
|
O
|
B:HOH745
|
3.7
|
21.7
|
1.0
|
OH
|
B:TYR107
|
4.0
|
6.2
|
1.0
|
OE2
|
B:GLU241
|
4.3
|
8.1
|
1.0
|
OD1
|
B:ASP198
|
4.4
|
6.1
|
1.0
|
O
|
B:GLY126
|
4.4
|
9.3
|
1.0
|
CE1
|
B:TYR107
|
4.5
|
7.8
|
1.0
|
CD
|
B:GLU241
|
4.5
|
7.5
|
1.0
|
CB
|
B:ASP113
|
4.5
|
5.7
|
1.0
|
CB
|
B:ASP109
|
4.5
|
6.7
|
1.0
|
CZ
|
B:TYR107
|
4.7
|
5.4
|
1.0
|
CA
|
B:CYS86
|
4.8
|
9.1
|
1.0
|
OE1
|
B:GLU241
|
4.8
|
8.1
|
1.0
|
OD2
|
B:ASP200
|
4.9
|
6.8
|
1.0
|
NE2
|
B:HIS196
|
4.9
|
8.1
|
1.0
|
CA
|
B:ASP198
|
5.0
|
6.4
|
1.0
|
CG
|
B:GLU241
|
5.0
|
7.8
|
1.0
|
O
|
B:HOH699
|
5.0
|
18.4
|
1.0
|
|
Manganese binding site 4 out
of 4 in 6luh
Go back to
Manganese Binding Sites List in 6luh
Manganese binding site 4 out
of 4 in the High Resolution Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 4 of High Resolution Structure of N(Omega)-Hydroxy-L-Arginine Hydrolase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn402
b:7.5
occ:1.00
|
O
|
B:HOH501
|
2.1
|
18.2
|
1.0
|
OD2
|
B:ASP200
|
2.1
|
6.8
|
1.0
|
OD2
|
B:ASP198
|
2.2
|
7.5
|
1.0
|
OD1
|
B:ASP109
|
2.2
|
5.7
|
1.0
|
O
|
B:HOH521
|
2.2
|
6.2
|
1.0
|
ND1
|
B:HIS111
|
2.2
|
6.6
|
1.0
|
OD1
|
B:ASP200
|
2.4
|
6.6
|
1.0
|
CG
|
B:ASP200
|
2.6
|
11.6
|
1.0
|
CG
|
B:ASP109
|
3.1
|
4.8
|
1.0
|
CE1
|
B:HIS111
|
3.1
|
5.7
|
1.0
|
CG
|
B:ASP198
|
3.1
|
8.2
|
1.0
|
CG
|
B:HIS111
|
3.3
|
6.7
|
1.0
|
O
|
B:HOH745
|
3.4
|
21.7
|
1.0
|
MN
|
B:MN401
|
3.4
|
6.7
|
1.0
|
OD2
|
B:ASP109
|
3.4
|
7.1
|
1.0
|
OD1
|
B:ASP198
|
3.6
|
6.1
|
1.0
|
CB
|
B:HIS111
|
3.7
|
5.7
|
1.0
|
N
|
B:HIS111
|
3.9
|
6.3
|
1.0
|
N
|
B:GLY110
|
4.1
|
7.0
|
1.0
|
CB
|
B:ASP200
|
4.1
|
9.4
|
1.0
|
O
|
B:HOH588
|
4.1
|
7.5
|
1.0
|
CB
|
B:ASP198
|
4.2
|
7.8
|
1.0
|
OD1
|
B:ASP113
|
4.3
|
6.9
|
1.0
|
NE2
|
B:HIS111
|
4.3
|
7.9
|
1.0
|
CD2
|
B:HIS111
|
4.4
|
7.4
|
1.0
|
CA
|
B:HIS111
|
4.4
|
8.6
|
1.0
|
CB
|
B:ASP109
|
4.5
|
6.7
|
1.0
|
O
|
B:HOH547
|
4.5
|
11.4
|
1.0
|
C
|
B:GLY110
|
4.6
|
7.7
|
1.0
|
O
|
B:HOH699
|
4.6
|
18.4
|
1.0
|
CA
|
B:GLY110
|
4.6
|
6.5
|
1.0
|
OD2
|
B:ASP113
|
4.7
|
4.0
|
1.0
|
CA
|
B:ASP109
|
4.8
|
6.8
|
1.0
|
C
|
B:ASP109
|
4.8
|
6.3
|
1.0
|
CG
|
B:ASP113
|
4.9
|
5.6
|
1.0
|
|
Reference:
K.Oda,
N.Shimotani,
T.Kuroda,
Y.Matoba.
Crystal Structure of An Nomega-Hydroxy-L-Arginine Hydrolase Found in the D-Cycloserine Biosynthetic Pathway. Acta Crystallogr D Struct V. 76 506 2020BIOL.
ISSN: ISSN 2059-7983
PubMed: 32496212
DOI: 10.1107/S2059798320004908
Page generated: Sun Oct 6 05:27:29 2024
|