Manganese in PDB 4cev: Arginase From Bacillus Caldevelox, L-Ornithine Complex
Enzymatic activity of Arginase From Bacillus Caldevelox, L-Ornithine Complex
All present enzymatic activity of Arginase From Bacillus Caldevelox, L-Ornithine Complex:
3.5.3.1;
Protein crystallography data
The structure of Arginase From Bacillus Caldevelox, L-Ornithine Complex, PDB code: 4cev
was solved by
M.C.Bewley,
P.D.Jeffrey,
M.L.Patchett,
Z.F.Kanyo,
E.N.Baker,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
8.00 /
2.70
|
Space group
|
C 2 2 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
106.600,
277.300,
139.700,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
20.3 /
27.4
|
Manganese Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
12;
Binding sites:
The binding sites of Manganese atom in the Arginase From Bacillus Caldevelox, L-Ornithine Complex
(pdb code 4cev). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 12 binding sites of Manganese where determined in the
Arginase From Bacillus Caldevelox, L-Ornithine Complex, PDB code: 4cev:
Jump to Manganese binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Manganese binding site 1 out
of 12 in 4cev
Go back to
Manganese Binding Sites List in 4cev
Manganese binding site 1 out
of 12 in the Arginase From Bacillus Caldevelox, L-Ornithine Complex
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Arginase From Bacillus Caldevelox, L-Ornithine Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn300
b:19.5
occ:1.00
|
O
|
A:HOH408
|
2.0
|
18.0
|
1.0
|
OD2
|
A:ASP122
|
2.1
|
12.5
|
1.0
|
ND1
|
A:HIS99
|
2.1
|
12.5
|
1.0
|
OD2
|
A:ASP126
|
2.2
|
26.2
|
1.0
|
OD2
|
A:ASP226
|
2.5
|
14.9
|
1.0
|
CG
|
A:ASP122
|
3.0
|
11.1
|
1.0
|
CE1
|
A:HIS99
|
3.1
|
16.3
|
1.0
|
CG
|
A:ASP126
|
3.1
|
18.3
|
1.0
|
CG
|
A:HIS99
|
3.2
|
11.5
|
1.0
|
MN
|
A:MN301
|
3.2
|
19.4
|
1.0
|
OD1
|
A:ASP122
|
3.2
|
10.1
|
1.0
|
OD1
|
A:ASP126
|
3.4
|
13.0
|
1.0
|
CG
|
A:ASP226
|
3.5
|
12.8
|
1.0
|
CB
|
A:HIS99
|
3.5
|
13.4
|
1.0
|
NE
|
A:ORN401
|
3.7
|
12.6
|
1.0
|
CB
|
A:ASP226
|
3.8
|
15.4
|
1.0
|
NE1
|
A:TRP120
|
4.2
|
5.4
|
1.0
|
NE2
|
A:HIS99
|
4.2
|
8.6
|
1.0
|
CD2
|
A:HIS99
|
4.3
|
6.7
|
1.0
|
CB
|
A:ASP122
|
4.4
|
9.6
|
1.0
|
CB
|
A:ASP126
|
4.5
|
17.4
|
1.0
|
O
|
A:HIS139
|
4.5
|
21.2
|
1.0
|
CD
|
A:ORN401
|
4.6
|
18.5
|
1.0
|
OD1
|
A:ASP226
|
4.6
|
13.3
|
1.0
|
ND1
|
A:HIS124
|
4.6
|
16.3
|
1.0
|
CB
|
A:HIS124
|
4.8
|
14.2
|
1.0
|
CE2
|
A:TRP120
|
4.8
|
12.8
|
1.0
|
OD2
|
A:ASP228
|
4.9
|
16.9
|
1.0
|
CZ2
|
A:TRP120
|
4.9
|
11.4
|
1.0
|
CG
|
A:GLU271
|
4.9
|
19.9
|
1.0
|
|
Manganese binding site 2 out
of 12 in 4cev
Go back to
Manganese Binding Sites List in 4cev
Manganese binding site 2 out
of 12 in the Arginase From Bacillus Caldevelox, L-Ornithine Complex
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Arginase From Bacillus Caldevelox, L-Ornithine Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn301
b:19.4
occ:1.00
|
OD1
|
A:ASP122
|
2.1
|
10.1
|
1.0
|
OD2
|
A:ASP228
|
2.2
|
16.9
|
1.0
|
ND1
|
A:HIS124
|
2.2
|
16.3
|
1.0
|
O
|
A:HOH408
|
2.2
|
18.0
|
1.0
|
OD2
|
A:ASP226
|
2.2
|
14.9
|
1.0
|
OD1
|
A:ASP228
|
2.3
|
20.5
|
1.0
|
CG
|
A:ASP228
|
2.6
|
17.7
|
1.0
|
CE1
|
A:HIS124
|
2.9
|
14.2
|
1.0
|
CG
|
A:ASP122
|
3.1
|
11.1
|
1.0
|
MN
|
A:MN300
|
3.2
|
19.5
|
1.0
|
CG
|
A:ASP226
|
3.2
|
12.8
|
1.0
|
CG
|
A:HIS124
|
3.4
|
16.1
|
1.0
|
OD2
|
A:ASP122
|
3.5
|
12.5
|
1.0
|
OD1
|
A:ASP226
|
3.8
|
13.3
|
1.0
|
CB
|
A:HIS124
|
3.9
|
14.2
|
1.0
|
N
|
A:HIS124
|
4.0
|
17.7
|
1.0
|
N
|
A:ALA123
|
4.1
|
7.3
|
1.0
|
CB
|
A:ASP228
|
4.1
|
15.9
|
1.0
|
NE2
|
A:HIS124
|
4.1
|
12.9
|
1.0
|
CB
|
A:ASP226
|
4.2
|
15.4
|
1.0
|
CD
|
A:ORN401
|
4.4
|
18.5
|
1.0
|
CD2
|
A:HIS124
|
4.4
|
12.0
|
1.0
|
NE
|
A:ORN401
|
4.4
|
12.6
|
1.0
|
CB
|
A:ASP122
|
4.4
|
9.6
|
1.0
|
CB
|
A:ALA123
|
4.5
|
7.7
|
1.0
|
CA
|
A:HIS124
|
4.6
|
15.2
|
1.0
|
OG1
|
A:THR240
|
4.6
|
33.1
|
1.0
|
CA
|
A:ALA123
|
4.7
|
12.2
|
1.0
|
C
|
A:ALA123
|
4.8
|
16.1
|
1.0
|
CA
|
A:ASP122
|
4.8
|
13.8
|
1.0
|
OD2
|
A:ASP126
|
4.9
|
26.2
|
1.0
|
C
|
A:ASP122
|
4.9
|
10.3
|
1.0
|
CA
|
A:ASP228
|
5.0
|
18.9
|
1.0
|
|
Manganese binding site 3 out
of 12 in 4cev
Go back to
Manganese Binding Sites List in 4cev
Manganese binding site 3 out
of 12 in the Arginase From Bacillus Caldevelox, L-Ornithine Complex
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 3 of Arginase From Bacillus Caldevelox, L-Ornithine Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn300
b:19.9
occ:1.00
|
O
|
A:HOH409
|
2.0
|
23.0
|
1.0
|
ND1
|
B:HIS99
|
2.1
|
13.4
|
1.0
|
OD2
|
B:ASP122
|
2.1
|
19.4
|
1.0
|
OD2
|
B:ASP126
|
2.2
|
18.9
|
1.0
|
OD2
|
B:ASP226
|
2.5
|
15.4
|
1.0
|
CG
|
B:ASP122
|
3.0
|
21.2
|
1.0
|
CE1
|
B:HIS99
|
3.0
|
12.3
|
1.0
|
CG
|
B:HIS99
|
3.1
|
15.1
|
1.0
|
CG
|
B:ASP126
|
3.1
|
15.6
|
1.0
|
MN
|
B:MN301
|
3.2
|
14.9
|
1.0
|
OD1
|
B:ASP122
|
3.2
|
16.4
|
1.0
|
OD1
|
B:ASP126
|
3.4
|
5.0
|
1.0
|
CB
|
B:HIS99
|
3.4
|
9.4
|
1.0
|
CG
|
B:ASP226
|
3.5
|
11.5
|
1.0
|
NE
|
A:ORN402
|
3.7
|
5.5
|
1.0
|
CB
|
B:ASP226
|
3.8
|
14.7
|
1.0
|
NE2
|
B:HIS99
|
4.1
|
12.0
|
1.0
|
CD2
|
B:HIS99
|
4.2
|
12.2
|
1.0
|
NE1
|
B:TRP120
|
4.2
|
17.5
|
1.0
|
CB
|
B:ASP122
|
4.4
|
14.1
|
1.0
|
O
|
B:HIS139
|
4.5
|
18.1
|
1.0
|
CB
|
B:ASP126
|
4.5
|
18.1
|
1.0
|
OD1
|
B:ASP226
|
4.5
|
13.0
|
1.0
|
ND1
|
B:HIS124
|
4.7
|
17.9
|
1.0
|
OD2
|
B:ASP228
|
4.8
|
11.6
|
1.0
|
CB
|
B:HIS124
|
4.8
|
15.0
|
1.0
|
CD
|
A:ORN402
|
4.9
|
18.2
|
1.0
|
CE2
|
B:TRP120
|
4.9
|
10.2
|
1.0
|
CZ2
|
B:TRP120
|
4.9
|
11.3
|
1.0
|
CG
|
B:GLU271
|
4.9
|
8.7
|
1.0
|
CA
|
B:HIS99
|
4.9
|
16.3
|
1.0
|
|
Manganese binding site 4 out
of 12 in 4cev
Go back to
Manganese Binding Sites List in 4cev
Manganese binding site 4 out
of 12 in the Arginase From Bacillus Caldevelox, L-Ornithine Complex
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 4 of Arginase From Bacillus Caldevelox, L-Ornithine Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn301
b:14.9
occ:1.00
|
OD1
|
B:ASP122
|
2.1
|
16.4
|
1.0
|
OD2
|
B:ASP228
|
2.2
|
11.6
|
1.0
|
O
|
A:HOH409
|
2.2
|
23.0
|
1.0
|
ND1
|
B:HIS124
|
2.2
|
17.9
|
1.0
|
OD2
|
B:ASP226
|
2.2
|
15.4
|
1.0
|
OD1
|
B:ASP228
|
2.3
|
23.2
|
1.0
|
CG
|
B:ASP228
|
2.6
|
19.2
|
1.0
|
CE1
|
B:HIS124
|
2.9
|
19.4
|
1.0
|
CG
|
B:ASP122
|
3.1
|
21.2
|
1.0
|
MN
|
B:MN300
|
3.2
|
19.9
|
1.0
|
CG
|
B:ASP226
|
3.2
|
11.5
|
1.0
|
CG
|
B:HIS124
|
3.3
|
14.6
|
1.0
|
OD2
|
B:ASP122
|
3.5
|
19.4
|
1.0
|
OD1
|
B:ASP226
|
3.8
|
13.0
|
1.0
|
CB
|
B:HIS124
|
3.8
|
15.0
|
1.0
|
N
|
B:HIS124
|
4.0
|
14.4
|
1.0
|
CB
|
B:ASP228
|
4.1
|
17.0
|
1.0
|
N
|
B:ALA123
|
4.1
|
15.9
|
1.0
|
NE2
|
B:HIS124
|
4.1
|
12.5
|
1.0
|
NE
|
A:ORN402
|
4.2
|
5.5
|
1.0
|
CB
|
B:ASP226
|
4.3
|
14.7
|
1.0
|
CD2
|
B:HIS124
|
4.4
|
9.2
|
1.0
|
CD
|
A:ORN402
|
4.4
|
18.2
|
1.0
|
CB
|
B:ASP122
|
4.5
|
14.1
|
1.0
|
OG1
|
B:THR240
|
4.6
|
28.2
|
1.0
|
CA
|
B:HIS124
|
4.6
|
15.6
|
1.0
|
O
|
B:HOH413
|
4.6
|
11.2
|
1.0
|
CB
|
B:ALA123
|
4.6
|
7.5
|
1.0
|
CA
|
B:ALA123
|
4.8
|
14.1
|
1.0
|
C
|
B:ALA123
|
4.8
|
15.2
|
1.0
|
OD2
|
B:ASP126
|
4.8
|
18.9
|
1.0
|
CA
|
B:ASP122
|
4.9
|
9.2
|
1.0
|
|
Manganese binding site 5 out
of 12 in 4cev
Go back to
Manganese Binding Sites List in 4cev
Manganese binding site 5 out
of 12 in the Arginase From Bacillus Caldevelox, L-Ornithine Complex
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 5 of Arginase From Bacillus Caldevelox, L-Ornithine Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn300
b:14.6
occ:1.00
|
O
|
A:HOH410
|
2.0
|
15.4
|
1.0
|
OD2
|
C:ASP122
|
2.1
|
14.4
|
1.0
|
ND1
|
C:HIS99
|
2.1
|
23.4
|
1.0
|
OD2
|
C:ASP126
|
2.2
|
24.1
|
1.0
|
OD2
|
C:ASP226
|
2.5
|
15.3
|
1.0
|
CG
|
C:ASP122
|
3.0
|
17.5
|
1.0
|
CE1
|
C:HIS99
|
3.1
|
27.9
|
1.0
|
CG
|
C:HIS99
|
3.1
|
20.8
|
1.0
|
CG
|
C:ASP126
|
3.1
|
21.5
|
1.0
|
MN
|
C:MN301
|
3.2
|
14.0
|
1.0
|
OD1
|
C:ASP122
|
3.3
|
13.1
|
1.0
|
OD1
|
C:ASP126
|
3.4
|
18.0
|
1.0
|
CB
|
C:HIS99
|
3.4
|
15.8
|
1.0
|
CG
|
C:ASP226
|
3.5
|
13.2
|
1.0
|
CB
|
C:ASP226
|
3.8
|
10.2
|
1.0
|
NE
|
A:ORN403
|
3.9
|
16.6
|
1.0
|
NE2
|
C:HIS99
|
4.2
|
20.3
|
1.0
|
CD2
|
C:HIS99
|
4.2
|
15.8
|
1.0
|
NE1
|
C:TRP120
|
4.2
|
16.7
|
1.0
|
CB
|
C:ASP122
|
4.4
|
17.0
|
1.0
|
CB
|
C:ASP126
|
4.5
|
22.8
|
1.0
|
O
|
C:HIS139
|
4.5
|
17.8
|
1.0
|
OD1
|
C:ASP226
|
4.6
|
14.1
|
1.0
|
ND1
|
C:HIS124
|
4.7
|
21.7
|
1.0
|
CB
|
C:HIS124
|
4.8
|
17.8
|
1.0
|
CE2
|
C:TRP120
|
4.9
|
16.1
|
1.0
|
CD
|
A:ORN403
|
4.9
|
17.1
|
1.0
|
CZ2
|
C:TRP120
|
4.9
|
13.4
|
1.0
|
OD2
|
C:ASP228
|
4.9
|
8.0
|
1.0
|
CA
|
C:HIS99
|
4.9
|
15.6
|
1.0
|
CG
|
C:GLU271
|
5.0
|
5.8
|
1.0
|
|
Manganese binding site 6 out
of 12 in 4cev
Go back to
Manganese Binding Sites List in 4cev
Manganese binding site 6 out
of 12 in the Arginase From Bacillus Caldevelox, L-Ornithine Complex
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 6 of Arginase From Bacillus Caldevelox, L-Ornithine Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn301
b:14.0
occ:1.00
|
OD1
|
C:ASP122
|
2.1
|
13.1
|
1.0
|
OD2
|
C:ASP228
|
2.2
|
8.0
|
1.0
|
O
|
A:HOH410
|
2.2
|
15.4
|
1.0
|
ND1
|
C:HIS124
|
2.2
|
21.7
|
1.0
|
OD2
|
C:ASP226
|
2.2
|
15.3
|
1.0
|
OD1
|
C:ASP228
|
2.3
|
18.1
|
1.0
|
CG
|
C:ASP228
|
2.6
|
17.9
|
1.0
|
CE1
|
C:HIS124
|
2.9
|
22.4
|
1.0
|
CG
|
C:ASP122
|
3.1
|
17.5
|
1.0
|
MN
|
C:MN300
|
3.2
|
14.6
|
1.0
|
CG
|
C:ASP226
|
3.2
|
13.2
|
1.0
|
CG
|
C:HIS124
|
3.4
|
21.1
|
1.0
|
OD2
|
C:ASP122
|
3.5
|
14.4
|
1.0
|
OD1
|
C:ASP226
|
3.8
|
14.1
|
1.0
|
CB
|
C:HIS124
|
3.9
|
17.8
|
1.0
|
N
|
C:HIS124
|
4.1
|
18.4
|
1.0
|
CB
|
C:ASP228
|
4.1
|
12.2
|
1.0
|
N
|
C:ALA123
|
4.1
|
19.9
|
1.0
|
NE2
|
C:HIS124
|
4.2
|
14.9
|
1.0
|
CB
|
C:ASP226
|
4.2
|
10.2
|
1.0
|
NE
|
A:ORN403
|
4.2
|
16.6
|
1.0
|
CD
|
A:ORN403
|
4.3
|
17.1
|
1.0
|
CD2
|
C:HIS124
|
4.4
|
17.1
|
1.0
|
OG1
|
C:THR240
|
4.5
|
33.4
|
1.0
|
O
|
C:HOH414
|
4.5
|
31.6
|
1.0
|
CB
|
C:ASP122
|
4.5
|
17.0
|
1.0
|
CA
|
C:HIS124
|
4.6
|
16.9
|
1.0
|
CB
|
C:ALA123
|
4.7
|
18.9
|
1.0
|
OD2
|
C:ASP126
|
4.8
|
24.1
|
1.0
|
CA
|
C:ALA123
|
4.8
|
19.5
|
1.0
|
C
|
C:ALA123
|
4.9
|
20.2
|
1.0
|
CA
|
C:ASP122
|
4.9
|
17.1
|
1.0
|
OD1
|
C:ASP126
|
4.9
|
18.0
|
1.0
|
CA
|
C:ASP228
|
5.0
|
12.2
|
1.0
|
|
Manganese binding site 7 out
of 12 in 4cev
Go back to
Manganese Binding Sites List in 4cev
Manganese binding site 7 out
of 12 in the Arginase From Bacillus Caldevelox, L-Ornithine Complex
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 7 of Arginase From Bacillus Caldevelox, L-Ornithine Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mn300
b:12.8
occ:1.00
|
O
|
A:HOH411
|
2.0
|
11.8
|
1.0
|
OD2
|
D:ASP122
|
2.1
|
13.1
|
1.0
|
ND1
|
D:HIS99
|
2.1
|
10.3
|
1.0
|
OD2
|
D:ASP126
|
2.2
|
19.0
|
1.0
|
OD2
|
D:ASP226
|
2.5
|
11.0
|
1.0
|
CG
|
D:ASP122
|
3.0
|
13.2
|
1.0
|
MN
|
D:MN301
|
3.0
|
12.3
|
1.0
|
CE1
|
D:HIS99
|
3.1
|
12.2
|
1.0
|
CG
|
D:ASP126
|
3.1
|
15.1
|
1.0
|
OD1
|
D:ASP122
|
3.1
|
13.9
|
1.0
|
CG
|
D:HIS99
|
3.2
|
14.4
|
1.0
|
OD1
|
D:ASP126
|
3.3
|
11.2
|
1.0
|
CG
|
D:ASP226
|
3.5
|
11.0
|
1.0
|
CB
|
D:HIS99
|
3.5
|
11.4
|
1.0
|
NE
|
A:ORN404
|
3.6
|
12.6
|
1.0
|
CB
|
D:ASP226
|
3.8
|
4.2
|
1.0
|
NE1
|
D:TRP120
|
4.1
|
5.0
|
1.0
|
NE2
|
D:HIS99
|
4.2
|
8.4
|
1.0
|
CD2
|
D:HIS99
|
4.3
|
6.4
|
1.0
|
CB
|
D:ASP122
|
4.3
|
9.1
|
1.0
|
O
|
D:HIS139
|
4.5
|
10.1
|
1.0
|
CB
|
D:ASP126
|
4.5
|
5.4
|
1.0
|
ND1
|
D:HIS124
|
4.6
|
10.6
|
1.0
|
OD1
|
D:ASP226
|
4.6
|
10.5
|
1.0
|
CB
|
D:HIS124
|
4.7
|
10.7
|
1.0
|
CD
|
A:ORN404
|
4.7
|
14.1
|
1.0
|
OD2
|
D:ASP228
|
4.8
|
8.3
|
1.0
|
CE2
|
D:TRP120
|
4.9
|
4.6
|
1.0
|
CZ2
|
D:TRP120
|
4.9
|
8.6
|
1.0
|
OD1
|
D:ASP228
|
4.9
|
11.8
|
1.0
|
CG
|
D:GLU271
|
5.0
|
5.8
|
1.0
|
|
Manganese binding site 8 out
of 12 in 4cev
Go back to
Manganese Binding Sites List in 4cev
Manganese binding site 8 out
of 12 in the Arginase From Bacillus Caldevelox, L-Ornithine Complex
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 8 of Arginase From Bacillus Caldevelox, L-Ornithine Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mn301
b:12.3
occ:1.00
|
OD1
|
D:ASP122
|
2.1
|
13.9
|
1.0
|
O
|
A:HOH411
|
2.2
|
11.8
|
1.0
|
OD2
|
D:ASP228
|
2.2
|
8.3
|
1.0
|
ND1
|
D:HIS124
|
2.2
|
10.6
|
1.0
|
OD2
|
D:ASP226
|
2.2
|
11.0
|
1.0
|
OD1
|
D:ASP228
|
2.4
|
11.8
|
1.0
|
CG
|
D:ASP228
|
2.6
|
13.0
|
1.0
|
CE1
|
D:HIS124
|
3.0
|
15.4
|
1.0
|
MN
|
D:MN300
|
3.0
|
12.8
|
1.0
|
CG
|
D:ASP122
|
3.1
|
13.2
|
1.0
|
CG
|
D:ASP226
|
3.2
|
11.0
|
1.0
|
CG
|
D:HIS124
|
3.4
|
12.8
|
1.0
|
OD2
|
D:ASP122
|
3.5
|
13.1
|
1.0
|
OD1
|
D:ASP226
|
3.8
|
10.5
|
1.0
|
CB
|
D:HIS124
|
3.8
|
10.7
|
1.0
|
N
|
D:HIS124
|
4.1
|
16.1
|
1.0
|
CB
|
D:ASP228
|
4.1
|
6.6
|
1.0
|
NE
|
A:ORN404
|
4.1
|
12.6
|
1.0
|
NE2
|
D:HIS124
|
4.2
|
7.4
|
1.0
|
N
|
D:ALA123
|
4.2
|
14.0
|
1.0
|
CB
|
D:ASP226
|
4.2
|
4.2
|
1.0
|
CD
|
A:ORN404
|
4.3
|
14.1
|
1.0
|
CD2
|
D:HIS124
|
4.4
|
12.6
|
1.0
|
CB
|
D:ASP122
|
4.5
|
9.1
|
1.0
|
OG1
|
D:THR240
|
4.5
|
30.5
|
1.0
|
CA
|
D:HIS124
|
4.6
|
15.1
|
1.0
|
CB
|
D:ALA123
|
4.7
|
16.2
|
1.0
|
OD2
|
D:ASP126
|
4.7
|
19.0
|
1.0
|
O
|
D:HOH415
|
4.8
|
24.1
|
1.0
|
CA
|
D:ASP122
|
4.9
|
10.9
|
1.0
|
CA
|
D:ALA123
|
4.9
|
16.6
|
1.0
|
C
|
D:ALA123
|
4.9
|
16.1
|
1.0
|
ND1
|
D:HIS99
|
4.9
|
10.3
|
1.0
|
OD1
|
D:ASP126
|
4.9
|
11.2
|
1.0
|
|
Manganese binding site 9 out
of 12 in 4cev
Go back to
Manganese Binding Sites List in 4cev
Manganese binding site 9 out
of 12 in the Arginase From Bacillus Caldevelox, L-Ornithine Complex
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 9 of Arginase From Bacillus Caldevelox, L-Ornithine Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mn300
b:19.7
occ:1.00
|
O
|
A:HOH412
|
2.0
|
15.4
|
1.0
|
ND1
|
E:HIS99
|
2.1
|
20.3
|
1.0
|
OD2
|
E:ASP122
|
2.1
|
13.4
|
1.0
|
OD2
|
E:ASP126
|
2.2
|
18.5
|
1.0
|
OD2
|
E:ASP226
|
2.5
|
16.4
|
1.0
|
CG
|
E:ASP122
|
3.0
|
21.8
|
1.0
|
CE1
|
E:HIS99
|
3.1
|
24.6
|
1.0
|
CG
|
E:HIS99
|
3.1
|
19.4
|
1.0
|
CG
|
E:ASP126
|
3.1
|
14.1
|
1.0
|
MN
|
E:MN301
|
3.1
|
16.7
|
1.0
|
OD1
|
E:ASP122
|
3.2
|
23.2
|
1.0
|
OD1
|
E:ASP126
|
3.3
|
24.2
|
1.0
|
CB
|
E:HIS99
|
3.4
|
20.4
|
1.0
|
CG
|
E:ASP226
|
3.5
|
18.3
|
1.0
|
NE
|
A:ORN405
|
3.8
|
24.1
|
1.0
|
CB
|
E:ASP226
|
3.8
|
18.6
|
1.0
|
NE2
|
E:HIS99
|
4.2
|
13.6
|
1.0
|
CD2
|
E:HIS99
|
4.2
|
18.2
|
1.0
|
NE1
|
E:TRP120
|
4.2
|
14.1
|
1.0
|
CB
|
E:ASP122
|
4.4
|
19.0
|
1.0
|
CB
|
E:ASP126
|
4.5
|
18.5
|
1.0
|
O
|
E:HIS139
|
4.5
|
15.6
|
1.0
|
OD1
|
E:ASP226
|
4.5
|
20.1
|
1.0
|
ND1
|
E:HIS124
|
4.6
|
19.9
|
1.0
|
CD
|
A:ORN405
|
4.8
|
23.5
|
1.0
|
CB
|
E:HIS124
|
4.8
|
19.2
|
1.0
|
OD2
|
E:ASP228
|
4.8
|
13.8
|
1.0
|
CG
|
E:GLU271
|
4.9
|
8.8
|
1.0
|
CA
|
E:HIS99
|
4.9
|
20.7
|
1.0
|
CE2
|
E:TRP120
|
4.9
|
10.5
|
1.0
|
CZ2
|
E:TRP120
|
4.9
|
7.3
|
1.0
|
OD1
|
E:ASP228
|
4.9
|
16.0
|
1.0
|
|
Manganese binding site 10 out
of 12 in 4cev
Go back to
Manganese Binding Sites List in 4cev
Manganese binding site 10 out
of 12 in the Arginase From Bacillus Caldevelox, L-Ornithine Complex
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 10 of Arginase From Bacillus Caldevelox, L-Ornithine Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mn301
b:16.7
occ:1.00
|
OD1
|
E:ASP122
|
2.1
|
23.2
|
1.0
|
ND1
|
E:HIS124
|
2.2
|
19.9
|
1.0
|
OD2
|
E:ASP228
|
2.2
|
13.8
|
1.0
|
O
|
A:HOH412
|
2.2
|
15.4
|
1.0
|
OD2
|
E:ASP226
|
2.2
|
16.4
|
1.0
|
OD1
|
E:ASP228
|
2.4
|
16.0
|
1.0
|
CG
|
E:ASP228
|
2.6
|
18.1
|
1.0
|
CE1
|
E:HIS124
|
2.9
|
15.5
|
1.0
|
CG
|
E:ASP122
|
3.1
|
21.8
|
1.0
|
MN
|
E:MN300
|
3.1
|
19.7
|
1.0
|
CG
|
E:ASP226
|
3.2
|
18.3
|
1.0
|
CG
|
E:HIS124
|
3.3
|
17.7
|
1.0
|
OD2
|
E:ASP122
|
3.5
|
13.4
|
1.0
|
CB
|
E:HIS124
|
3.8
|
19.2
|
1.0
|
OD1
|
E:ASP226
|
3.9
|
20.1
|
1.0
|
N
|
E:HIS124
|
4.0
|
15.6
|
1.0
|
CB
|
E:ASP228
|
4.1
|
18.1
|
1.0
|
NE2
|
E:HIS124
|
4.1
|
15.5
|
1.0
|
N
|
E:ALA123
|
4.1
|
12.4
|
1.0
|
CB
|
E:ASP226
|
4.2
|
18.6
|
1.0
|
NE
|
A:ORN405
|
4.3
|
24.1
|
1.0
|
CD2
|
E:HIS124
|
4.4
|
12.9
|
1.0
|
CD
|
A:ORN405
|
4.4
|
23.5
|
1.0
|
CB
|
E:ASP122
|
4.4
|
19.0
|
1.0
|
CA
|
E:HIS124
|
4.5
|
18.4
|
1.0
|
CB
|
E:ALA123
|
4.6
|
14.8
|
1.0
|
OG1
|
E:THR240
|
4.6
|
36.8
|
1.0
|
O
|
E:HOH306
|
4.7
|
8.1
|
1.0
|
OD2
|
E:ASP126
|
4.8
|
18.5
|
1.0
|
CA
|
E:ALA123
|
4.8
|
13.0
|
1.0
|
C
|
E:ALA123
|
4.8
|
11.5
|
1.0
|
CA
|
E:ASP122
|
4.8
|
17.3
|
1.0
|
OD1
|
E:ASP126
|
4.9
|
24.2
|
1.0
|
ND1
|
E:HIS99
|
5.0
|
20.3
|
1.0
|
C
|
E:ASP122
|
5.0
|
14.6
|
1.0
|
|
Reference:
M.C.Bewley,
P.D.Jeffrey,
M.L.Patchett,
Z.F.Kanyo,
E.N.Baker.
Crystal Structures of Bacillus Caldovelox Arginase in Complex with Substrate and Inhibitors Reveal New Insights Into Activation, Inhibition and Catalysis in the Arginase Superfamily. Structure Fold.Des. V. 7 435 1999.
ISSN: ISSN 0969-2126
PubMed: 10196128
DOI: 10.1016/S0969-2126(99)80056-2
Page generated: Sat Oct 5 18:54:38 2024
|