Manganese in PDB 1jdb: Carbamoyl Phosphate Synthetase From Escherichia Coli
Enzymatic activity of Carbamoyl Phosphate Synthetase From Escherichia Coli
All present enzymatic activity of Carbamoyl Phosphate Synthetase From Escherichia Coli:
6.3.5.5;
Protein crystallography data
The structure of Carbamoyl Phosphate Synthetase From Escherichia Coli, PDB code: 1jdb
was solved by
J.B.Thoden,
H.M.Holden,
G.Wesenberg,
F.M.Raushel,
I.Rayment,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
30.00 /
2.10
|
|
Space group
|
P 21 21 21
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
143.800,
167.700,
323.000,
90.00,
90.00,
90.00
|
|
R / Rfree (%)
|
17.9 /
n/a
|
Other elements in 1jdb:
The structure of Carbamoyl Phosphate Synthetase From Escherichia Coli also contains other interesting chemical elements:
Manganese Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
16;
Binding sites:
The binding sites of Manganese atom in the Carbamoyl Phosphate Synthetase From Escherichia Coli
(pdb code 1jdb). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 16 binding sites of Manganese where determined in the
Carbamoyl Phosphate Synthetase From Escherichia Coli, PDB code: 1jdb:
Jump to Manganese binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Manganese binding site 1 out
of 16 in 1jdb
Go back to
Manganese Binding Sites List in 1jdb
Manganese binding site 1 out
of 16 in the Carbamoyl Phosphate Synthetase From Escherichia Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Carbamoyl Phosphate Synthetase From Escherichia Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn1073
b:15.8
occ:1.00
|
O3B
|
B:ADP1093
|
2.0
|
10.7
|
1.0
|
|
O1
|
B:PO41078
|
2.1
|
15.7
|
1.0
|
|
OD1
|
B:ASN300
|
2.1
|
15.3
|
1.0
|
|
OE1
|
B:GLU298
|
2.3
|
12.7
|
1.0
|
|
O
|
B:HOH1097
|
2.4
|
23.5
|
1.0
|
|
OE2
|
B:GLU298
|
2.4
|
13.8
|
1.0
|
|
CD
|
B:GLU298
|
2.7
|
23.6
|
1.0
|
|
CG
|
B:ASN300
|
3.1
|
27.9
|
1.0
|
|
PB
|
B:ADP1093
|
3.3
|
10.8
|
1.0
|
|
P
|
B:PO41078
|
3.4
|
14.6
|
1.0
|
|
O1B
|
B:ADP1093
|
3.4
|
14.6
|
1.0
|
|
ND2
|
B:ASN300
|
3.5
|
13.3
|
1.0
|
|
O3
|
B:PO41078
|
3.6
|
6.5
|
1.0
|
|
MN
|
B:MN1074
|
3.6
|
14.2
|
1.0
|
|
CB
|
B:MET173
|
3.7
|
10.2
|
1.0
|
|
K
|
B:K1076
|
3.8
|
17.1
|
1.0
|
|
NH2
|
B:ARG128
|
4.1
|
17.2
|
1.0
|
|
O
|
B:HOH1256
|
4.1
|
9.8
|
1.0
|
|
NH2
|
B:ARG302
|
4.1
|
9.7
|
1.0
|
|
O3A
|
B:ADP1093
|
4.2
|
21.0
|
1.0
|
|
CG
|
B:GLU298
|
4.2
|
5.1
|
1.0
|
|
CA
|
B:MET173
|
4.2
|
20.1
|
1.0
|
|
O2
|
B:PO41078
|
4.3
|
15.8
|
1.0
|
|
O4
|
B:PO41078
|
4.3
|
14.4
|
1.0
|
|
O2B
|
B:ADP1093
|
4.3
|
13.2
|
1.0
|
|
O
|
B:THR172
|
4.4
|
14.1
|
1.0
|
|
CB
|
B:ASN300
|
4.4
|
10.6
|
1.0
|
|
O1A
|
B:ADP1093
|
4.5
|
17.9
|
1.0
|
|
O
|
B:HOH1162
|
4.8
|
23.5
|
1.0
|
|
PA
|
B:ADP1093
|
4.9
|
14.4
|
1.0
|
|
CB
|
B:GLU298
|
5.0
|
7.0
|
1.0
|
|
NH1
|
B:ARG128
|
5.0
|
15.0
|
1.0
|
|
Manganese binding site 2 out
of 16 in 1jdb
Go back to
Manganese Binding Sites List in 1jdb
Manganese binding site 2 out
of 16 in the Carbamoyl Phosphate Synthetase From Escherichia Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Carbamoyl Phosphate Synthetase From Escherichia Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn1074
b:14.2
occ:1.00
|
O3
|
B:PO41078
|
2.0
|
6.5
|
1.0
|
|
O1A
|
B:ADP1093
|
2.1
|
17.9
|
1.0
|
|
OE2
|
B:GLU298
|
2.2
|
13.8
|
1.0
|
|
O1B
|
B:ADP1093
|
2.2
|
14.6
|
1.0
|
|
OE1
|
B:GLN284
|
2.3
|
13.8
|
1.0
|
|
O
|
B:HOH1098
|
2.4
|
16.2
|
1.0
|
|
PB
|
B:ADP1093
|
3.2
|
10.8
|
1.0
|
|
P
|
B:PO41078
|
3.2
|
14.6
|
1.0
|
|
CD
|
B:GLN284
|
3.2
|
13.3
|
1.0
|
|
CD
|
B:GLU298
|
3.3
|
23.6
|
1.0
|
|
PA
|
B:ADP1093
|
3.4
|
14.4
|
1.0
|
|
O1
|
B:PO41078
|
3.5
|
15.7
|
1.0
|
|
O3A
|
B:ADP1093
|
3.5
|
21.0
|
1.0
|
|
NE2
|
B:GLN284
|
3.6
|
9.8
|
1.0
|
|
O3B
|
B:ADP1093
|
3.6
|
10.7
|
1.0
|
|
MN
|
B:MN1073
|
3.6
|
15.8
|
1.0
|
|
K
|
B:K1077
|
3.6
|
28.2
|
1.0
|
|
O4
|
B:PO41078
|
3.8
|
14.4
|
1.0
|
|
NE2
|
B:HIS242
|
3.9
|
9.3
|
1.0
|
|
CG
|
B:GLU298
|
3.9
|
5.1
|
1.0
|
|
OE1
|
B:GLU298
|
4.2
|
12.7
|
1.0
|
|
ND2
|
B:ASN300
|
4.3
|
13.3
|
1.0
|
|
CE1
|
B:HIS242
|
4.3
|
6.8
|
1.0
|
|
O2A
|
B:ADP1093
|
4.4
|
4.0
|
1.0
|
|
O5'
|
B:ADP1093
|
4.4
|
9.2
|
1.0
|
|
O2
|
B:PO41078
|
4.4
|
15.8
|
1.0
|
|
C5'
|
B:ADP1093
|
4.5
|
1.0
|
1.0
|
|
O3'
|
B:ADP1093
|
4.5
|
10.1
|
1.0
|
|
O2B
|
B:ADP1093
|
4.5
|
13.2
|
1.0
|
|
CG
|
B:GLN284
|
4.6
|
12.1
|
1.0
|
|
OG1
|
B:THR243
|
4.7
|
10.8
|
1.0
|
|
CD2
|
B:HIS242
|
4.8
|
1.7
|
1.0
|
|
OD1
|
B:ASN300
|
4.9
|
15.3
|
1.0
|
|
C3'
|
B:ADP1093
|
5.0
|
12.7
|
1.0
|
|
Manganese binding site 3 out
of 16 in 1jdb
Go back to
Manganese Binding Sites List in 1jdb
Manganese binding site 3 out
of 16 in the Carbamoyl Phosphate Synthetase From Escherichia Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 3 of Carbamoyl Phosphate Synthetase From Escherichia Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn1079
b:36.6
occ:1.00
|
OE2
|
B:GLU840
|
1.9
|
31.6
|
1.0
|
|
O2A
|
B:ADP1094
|
2.0
|
25.3
|
1.0
|
|
O3B
|
B:ADP1094
|
2.0
|
26.9
|
1.0
|
|
OE1
|
B:GLN828
|
2.1
|
34.4
|
1.0
|
|
O
|
B:HOH1108
|
2.3
|
29.1
|
1.0
|
|
O
|
B:HOH1107
|
2.4
|
33.6
|
1.0
|
|
CD
|
B:GLU840
|
3.0
|
62.6
|
1.0
|
|
CD
|
B:GLN828
|
3.0
|
35.2
|
1.0
|
|
NE2
|
B:GLN828
|
3.3
|
43.4
|
1.0
|
|
PA
|
B:ADP1094
|
3.3
|
32.7
|
1.0
|
|
PB
|
B:ADP1094
|
3.4
|
24.6
|
1.0
|
|
O3A
|
B:ADP1094
|
3.7
|
32.9
|
1.0
|
|
CG
|
B:GLU840
|
3.7
|
29.1
|
1.0
|
|
OE1
|
B:GLU840
|
3.7
|
28.8
|
1.0
|
|
MN
|
B:MN1080
|
3.9
|
67.7
|
1.0
|
|
O5'
|
B:ADP1094
|
4.1
|
25.9
|
1.0
|
|
OG
|
B:SER788
|
4.2
|
38.8
|
1.0
|
|
O2B
|
B:ADP1094
|
4.3
|
55.0
|
1.0
|
|
O1A
|
B:ADP1094
|
4.3
|
33.8
|
1.0
|
|
O
|
B:HOH1111
|
4.3
|
33.0
|
1.0
|
|
C5'
|
B:ADP1094
|
4.3
|
21.3
|
1.0
|
|
O3'
|
B:ADP1094
|
4.4
|
15.7
|
1.0
|
|
O1B
|
B:ADP1094
|
4.4
|
30.1
|
1.0
|
|
ND2
|
B:ASN842
|
4.4
|
54.5
|
1.0
|
|
CG
|
B:GLN828
|
4.5
|
20.9
|
1.0
|
|
NE2
|
B:HIS787
|
4.6
|
20.9
|
1.0
|
|
O
|
B:HOH1914
|
4.7
|
38.6
|
1.0
|
|
CE1
|
B:HIS787
|
4.7
|
25.8
|
1.0
|
|
C3'
|
B:ADP1094
|
4.8
|
16.2
|
1.0
|
|
OD1
|
B:ASN842
|
5.0
|
32.6
|
1.0
|
|
CB
|
B:GLN828
|
5.0
|
21.9
|
1.0
|
|
CB
|
B:GLU840
|
5.0
|
33.7
|
1.0
|
|
Manganese binding site 4 out
of 16 in 1jdb
Go back to
Manganese Binding Sites List in 1jdb
Manganese binding site 4 out
of 16 in the Carbamoyl Phosphate Synthetase From Escherichia Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 4 of Carbamoyl Phosphate Synthetase From Escherichia Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn1080
b:67.7
occ:1.00
|
O2B
|
B:ADP1094
|
2.6
|
55.0
|
1.0
|
|
OE1
|
B:GLU840
|
2.7
|
28.8
|
1.0
|
|
O
|
B:HOH1109
|
2.9
|
59.1
|
1.0
|
|
O3B
|
B:ADP1094
|
2.9
|
26.9
|
1.0
|
|
OE2
|
B:GLU840
|
3.0
|
31.6
|
1.0
|
|
OD1
|
B:ASN842
|
3.1
|
32.6
|
1.0
|
|
CD
|
B:GLU840
|
3.2
|
62.6
|
1.0
|
|
PB
|
B:ADP1094
|
3.4
|
24.6
|
1.0
|
|
MN
|
B:MN1079
|
3.9
|
36.6
|
1.0
|
|
O
|
B:HOH1107
|
3.9
|
33.6
|
1.0
|
|
CG
|
B:ASN842
|
4.0
|
0.0
|
1.0
|
|
O
|
B:HOH1111
|
4.1
|
33.0
|
1.0
|
|
O
|
B:HOH1110
|
4.2
|
31.5
|
1.0
|
|
O
|
B:HOH1700
|
4.3
|
29.7
|
1.0
|
|
ND2
|
B:ASN842
|
4.4
|
54.5
|
1.0
|
|
NH2
|
B:ARG844
|
4.4
|
0.0
|
1.0
|
|
O1B
|
B:ADP1094
|
4.5
|
30.1
|
1.0
|
|
O2A
|
B:ADP1094
|
4.5
|
25.3
|
1.0
|
|
O3A
|
B:ADP1094
|
4.5
|
32.9
|
1.0
|
|
CG
|
B:GLU840
|
4.7
|
29.1
|
1.0
|
|
Manganese binding site 5 out
of 16 in 1jdb
Go back to
Manganese Binding Sites List in 1jdb
Manganese binding site 5 out
of 16 in the Carbamoyl Phosphate Synthetase From Escherichia Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 5 of Carbamoyl Phosphate Synthetase From Escherichia Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mn1073
b:15.7
occ:1.00
|
O1
|
E:PO41078
|
2.0
|
9.6
|
1.0
|
|
O3B
|
E:ADP1095
|
2.2
|
17.8
|
1.0
|
|
O
|
E:HOH1215
|
2.2
|
21.8
|
1.0
|
|
OE1
|
E:GLU298
|
2.2
|
12.8
|
1.0
|
|
OE2
|
E:GLU298
|
2.3
|
8.0
|
1.0
|
|
OD1
|
E:ASN300
|
2.4
|
14.8
|
1.0
|
|
CD
|
E:GLU298
|
2.6
|
11.5
|
1.0
|
|
CG
|
E:ASN300
|
3.2
|
19.4
|
1.0
|
|
O1B
|
E:ADP1095
|
3.2
|
13.3
|
1.0
|
|
PB
|
E:ADP1095
|
3.2
|
16.0
|
1.0
|
|
P
|
E:PO41078
|
3.3
|
16.7
|
1.0
|
|
ND2
|
E:ASN300
|
3.3
|
18.2
|
1.0
|
|
O3
|
E:PO41078
|
3.6
|
7.5
|
1.0
|
|
MN
|
E:MN1074
|
3.6
|
14.8
|
1.0
|
|
CB
|
E:MET173
|
3.8
|
10.5
|
1.0
|
|
K
|
E:K1076
|
3.9
|
18.7
|
1.0
|
|
CG
|
E:GLU298
|
4.1
|
10.6
|
1.0
|
|
NH2
|
E:ARG302
|
4.1
|
10.2
|
1.0
|
|
O4
|
E:PO41078
|
4.1
|
12.9
|
1.0
|
|
O3A
|
E:ADP1095
|
4.2
|
16.7
|
1.0
|
|
O2
|
E:PO41078
|
4.3
|
9.5
|
1.0
|
|
O2B
|
E:ADP1095
|
4.3
|
22.1
|
1.0
|
|
CA
|
E:MET173
|
4.3
|
13.9
|
1.0
|
|
O
|
E:HOH1372
|
4.3
|
13.9
|
1.0
|
|
NH2
|
E:ARG128
|
4.3
|
20.1
|
1.0
|
|
O
|
E:THR172
|
4.4
|
12.0
|
1.0
|
|
O1A
|
E:ADP1095
|
4.5
|
12.6
|
1.0
|
|
CB
|
E:ASN300
|
4.6
|
9.8
|
1.0
|
|
PA
|
E:ADP1095
|
4.9
|
17.6
|
1.0
|
|
NH1
|
E:ARG128
|
4.9
|
14.7
|
1.0
|
|
OE1
|
E:GLN284
|
4.9
|
26.6
|
1.0
|
|
Manganese binding site 6 out
of 16 in 1jdb
Go back to
Manganese Binding Sites List in 1jdb
Manganese binding site 6 out
of 16 in the Carbamoyl Phosphate Synthetase From Escherichia Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 6 of Carbamoyl Phosphate Synthetase From Escherichia Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mn1074
b:14.8
occ:1.00
|
O3
|
E:PO41078
|
2.1
|
7.5
|
1.0
|
|
OE1
|
E:GLN284
|
2.1
|
26.6
|
1.0
|
|
O1A
|
E:ADP1095
|
2.1
|
12.6
|
1.0
|
|
O1B
|
E:ADP1095
|
2.2
|
13.3
|
1.0
|
|
OE2
|
E:GLU298
|
2.2
|
8.0
|
1.0
|
|
O
|
E:HOH1216
|
2.4
|
13.9
|
1.0
|
|
CD
|
E:GLN284
|
3.0
|
30.6
|
1.0
|
|
P
|
E:PO41078
|
3.2
|
16.7
|
1.0
|
|
NE2
|
E:GLN284
|
3.3
|
12.8
|
1.0
|
|
PB
|
E:ADP1095
|
3.3
|
16.0
|
1.0
|
|
CD
|
E:GLU298
|
3.3
|
11.5
|
1.0
|
|
PA
|
E:ADP1095
|
3.4
|
17.6
|
1.0
|
|
O1
|
E:PO41078
|
3.5
|
9.6
|
1.0
|
|
MN
|
E:MN1073
|
3.6
|
15.7
|
1.0
|
|
O3A
|
E:ADP1095
|
3.6
|
16.7
|
1.0
|
|
K
|
E:K1077
|
3.6
|
28.2
|
1.0
|
|
O3B
|
E:ADP1095
|
3.8
|
17.8
|
1.0
|
|
O4
|
E:PO41078
|
3.8
|
12.9
|
1.0
|
|
NE2
|
E:HIS242
|
3.9
|
10.9
|
1.0
|
|
CG
|
E:GLU298
|
4.0
|
10.6
|
1.0
|
|
OE1
|
E:GLU298
|
4.1
|
12.8
|
1.0
|
|
ND2
|
E:ASN300
|
4.2
|
18.2
|
1.0
|
|
CE1
|
E:HIS242
|
4.3
|
16.1
|
1.0
|
|
CG
|
E:GLN284
|
4.4
|
15.7
|
1.0
|
|
O2A
|
E:ADP1095
|
4.4
|
12.8
|
1.0
|
|
O5'
|
E:ADP1095
|
4.4
|
14.7
|
1.0
|
|
C5'
|
E:ADP1095
|
4.4
|
2.7
|
1.0
|
|
O2
|
E:PO41078
|
4.5
|
9.5
|
1.0
|
|
O3'
|
E:ADP1095
|
4.5
|
13.4
|
1.0
|
|
OG1
|
E:THR243
|
4.5
|
14.0
|
1.0
|
|
O2B
|
E:ADP1095
|
4.6
|
22.1
|
1.0
|
|
CD2
|
E:HIS242
|
4.8
|
12.7
|
1.0
|
|
Manganese binding site 7 out
of 16 in 1jdb
Go back to
Manganese Binding Sites List in 1jdb
Manganese binding site 7 out
of 16 in the Carbamoyl Phosphate Synthetase From Escherichia Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 7 of Carbamoyl Phosphate Synthetase From Escherichia Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mn1079
b:20.2
occ:1.00
|
OE2
|
E:GLU840
|
1.9
|
13.3
|
1.0
|
|
O2A
|
E:ADP1096
|
2.1
|
39.3
|
1.0
|
|
OE1
|
E:GLN828
|
2.1
|
14.9
|
1.0
|
|
O3B
|
E:ADP1096
|
2.1
|
20.8
|
1.0
|
|
O
|
E:HOH1225
|
2.1
|
13.8
|
1.0
|
|
O
|
E:HOH1226
|
2.2
|
21.5
|
1.0
|
|
CD
|
E:GLN828
|
3.0
|
52.9
|
1.0
|
|
CD
|
E:GLU840
|
3.1
|
29.1
|
1.0
|
|
PA
|
E:ADP1096
|
3.3
|
21.6
|
1.0
|
|
PB
|
E:ADP1096
|
3.3
|
23.1
|
1.0
|
|
NE2
|
E:GLN828
|
3.4
|
21.8
|
1.0
|
|
O3A
|
E:ADP1096
|
3.6
|
26.7
|
1.0
|
|
O
|
E:HOH1230
|
3.6
|
22.6
|
1.0
|
|
MN
|
E:MN1080
|
3.7
|
43.0
|
1.0
|
|
OE1
|
E:GLU840
|
3.9
|
22.6
|
1.0
|
|
CG
|
E:GLU840
|
3.9
|
24.1
|
1.0
|
|
O2B
|
E:ADP1096
|
4.2
|
33.1
|
1.0
|
|
O5'
|
E:ADP1096
|
4.2
|
18.5
|
1.0
|
|
C5'
|
E:ADP1096
|
4.3
|
14.9
|
1.0
|
|
O1A
|
E:ADP1096
|
4.3
|
26.4
|
1.0
|
|
OG
|
E:SER788
|
4.4
|
24.4
|
1.0
|
|
CG
|
E:GLN828
|
4.4
|
29.8
|
1.0
|
|
ND2
|
E:ASN842
|
4.4
|
17.2
|
1.0
|
|
O3'
|
E:ADP1096
|
4.4
|
15.3
|
1.0
|
|
O1B
|
E:ADP1096
|
4.4
|
27.7
|
1.0
|
|
O
|
E:HOH2226
|
4.5
|
23.9
|
1.0
|
|
NE2
|
E:HIS787
|
4.7
|
13.1
|
1.0
|
|
C3'
|
E:ADP1096
|
4.8
|
11.3
|
1.0
|
|
CE1
|
E:HIS787
|
4.9
|
17.3
|
1.0
|
|
OD1
|
E:ASN842
|
5.0
|
20.6
|
1.0
|
|
Manganese binding site 8 out
of 16 in 1jdb
Go back to
Manganese Binding Sites List in 1jdb
Manganese binding site 8 out
of 16 in the Carbamoyl Phosphate Synthetase From Escherichia Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 8 of Carbamoyl Phosphate Synthetase From Escherichia Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mn1080
b:43.0
occ:1.00
|
OD1
|
E:ASN842
|
2.6
|
20.6
|
1.0
|
|
OE1
|
E:GLU840
|
2.7
|
22.6
|
1.0
|
|
OE2
|
E:GLU840
|
2.7
|
13.3
|
1.0
|
|
O2B
|
E:ADP1096
|
2.8
|
33.1
|
1.0
|
|
O3B
|
E:ADP1096
|
3.0
|
20.8
|
1.0
|
|
O
|
E:HOH1227
|
3.0
|
49.3
|
1.0
|
|
CD
|
E:GLU840
|
3.0
|
29.1
|
1.0
|
|
O
|
E:HOH1230
|
3.4
|
22.6
|
1.0
|
|
PB
|
E:ADP1096
|
3.4
|
23.1
|
1.0
|
|
CG
|
E:ASN842
|
3.5
|
17.4
|
1.0
|
|
O
|
E:HOH1225
|
3.7
|
13.8
|
1.0
|
|
MN
|
E:MN1079
|
3.7
|
20.2
|
1.0
|
|
O
|
E:HOH1228
|
3.9
|
37.3
|
1.0
|
|
ND2
|
E:ASN842
|
3.9
|
17.2
|
1.0
|
|
O
|
E:HOH2295
|
4.0
|
42.9
|
1.0
|
|
K
|
E:K1085
|
4.1
|
31.5
|
1.0
|
|
NH2
|
E:ARG844
|
4.1
|
0.0
|
1.0
|
|
O
|
E:HOH2080
|
4.2
|
31.0
|
1.0
|
|
CG
|
E:GLU840
|
4.4
|
24.1
|
1.0
|
|
O1B
|
E:ADP1096
|
4.5
|
27.7
|
1.0
|
|
O3A
|
E:ADP1096
|
4.6
|
26.7
|
1.0
|
|
O2A
|
E:ADP1096
|
4.7
|
39.3
|
1.0
|
|
CB
|
E:ASN842
|
4.8
|
6.4
|
1.0
|
|
Manganese binding site 9 out
of 16 in 1jdb
Go back to
Manganese Binding Sites List in 1jdb
Manganese binding site 9 out
of 16 in the Carbamoyl Phosphate Synthetase From Escherichia Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 9 of Carbamoyl Phosphate Synthetase From Escherichia Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Mn1073
b:19.2
occ:1.00
|
O1
|
H:PO41078
|
2.0
|
4.8
|
1.0
|
|
O
|
H:HOH1107
|
2.1
|
18.3
|
1.0
|
|
O3B
|
H:ADP1092
|
2.2
|
24.8
|
1.0
|
|
OE1
|
H:GLU298
|
2.3
|
17.0
|
1.0
|
|
OD1
|
H:ASN300
|
2.3
|
23.7
|
1.0
|
|
OE2
|
H:GLU298
|
2.4
|
19.0
|
1.0
|
|
CD
|
H:GLU298
|
2.7
|
26.7
|
1.0
|
|
CG
|
H:ASN300
|
3.1
|
26.7
|
1.0
|
|
PB
|
H:ADP1092
|
3.3
|
14.9
|
1.0
|
|
ND2
|
H:ASN300
|
3.3
|
15.2
|
1.0
|
|
P
|
H:PO41078
|
3.3
|
19.1
|
1.0
|
|
O1B
|
H:ADP1092
|
3.4
|
12.8
|
1.0
|
|
O3
|
H:PO41078
|
3.6
|
15.7
|
1.0
|
|
MN
|
H:MN1074
|
3.7
|
17.8
|
1.0
|
|
K
|
H:K1076
|
3.8
|
18.6
|
1.0
|
|
CB
|
H:MET173
|
4.0
|
17.1
|
1.0
|
|
NH2
|
H:ARG302
|
4.1
|
18.1
|
1.0
|
|
O
|
H:HOH1264
|
4.2
|
14.9
|
1.0
|
|
CG
|
H:GLU298
|
4.2
|
5.5
|
1.0
|
|
O2
|
H:PO41078
|
4.2
|
16.2
|
1.0
|
|
CA
|
H:MET173
|
4.2
|
25.6
|
1.0
|
|
O3A
|
H:ADP1092
|
4.3
|
25.2
|
1.0
|
|
O
|
H:THR172
|
4.3
|
19.6
|
1.0
|
|
O4
|
H:PO41078
|
4.3
|
15.9
|
1.0
|
|
O2B
|
H:ADP1092
|
4.3
|
23.9
|
1.0
|
|
NH2
|
H:ARG128
|
4.4
|
17.2
|
1.0
|
|
O1A
|
H:ADP1092
|
4.4
|
12.2
|
1.0
|
|
CB
|
H:ASN300
|
4.5
|
9.4
|
1.0
|
|
NH1
|
H:ARG128
|
4.8
|
19.6
|
1.0
|
|
PA
|
H:ADP1092
|
4.9
|
18.7
|
1.0
|
|
O
|
H:HOH1171
|
4.9
|
24.5
|
1.0
|
|
OE1
|
H:GLN284
|
5.0
|
13.0
|
1.0
|
|
Manganese binding site 10 out
of 16 in 1jdb
Go back to
Manganese Binding Sites List in 1jdb
Manganese binding site 10 out
of 16 in the Carbamoyl Phosphate Synthetase From Escherichia Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 10 of Carbamoyl Phosphate Synthetase From Escherichia Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Mn1074
b:17.8
occ:1.00
|
O1A
|
H:ADP1092
|
2.0
|
12.2
|
1.0
|
|
O3
|
H:PO41078
|
2.1
|
15.7
|
1.0
|
|
O1B
|
H:ADP1092
|
2.2
|
12.8
|
1.0
|
|
OE1
|
H:GLN284
|
2.2
|
13.0
|
1.0
|
|
OE2
|
H:GLU298
|
2.3
|
19.0
|
1.0
|
|
O
|
H:HOH1108
|
2.3
|
15.8
|
1.0
|
|
CD
|
H:GLN284
|
3.1
|
20.1
|
1.0
|
|
PB
|
H:ADP1092
|
3.2
|
14.9
|
1.0
|
|
NE2
|
H:GLN284
|
3.3
|
22.9
|
1.0
|
|
PA
|
H:ADP1092
|
3.3
|
18.7
|
1.0
|
|
P
|
H:PO41078
|
3.3
|
19.1
|
1.0
|
|
CD
|
H:GLU298
|
3.4
|
26.7
|
1.0
|
|
O1
|
H:PO41078
|
3.5
|
4.8
|
1.0
|
|
K
|
H:K1077
|
3.6
|
33.6
|
1.0
|
|
O3A
|
H:ADP1092
|
3.6
|
25.2
|
1.0
|
|
MN
|
H:MN1073
|
3.7
|
19.2
|
1.0
|
|
O3B
|
H:ADP1092
|
3.8
|
24.8
|
1.0
|
|
NE2
|
H:HIS242
|
3.9
|
14.3
|
1.0
|
|
O4
|
H:PO41078
|
4.0
|
15.9
|
1.0
|
|
CG
|
H:GLU298
|
4.1
|
5.5
|
1.0
|
|
ND2
|
H:ASN300
|
4.1
|
15.2
|
1.0
|
|
OE1
|
H:GLU298
|
4.1
|
17.0
|
1.0
|
|
CE1
|
H:HIS242
|
4.3
|
6.6
|
1.0
|
|
O2A
|
H:ADP1092
|
4.3
|
8.7
|
1.0
|
|
O5'
|
H:ADP1092
|
4.3
|
19.2
|
1.0
|
|
C5'
|
H:ADP1092
|
4.4
|
7.0
|
1.0
|
|
O3'
|
H:ADP1092
|
4.4
|
13.8
|
1.0
|
|
OG1
|
H:THR243
|
4.4
|
14.7
|
1.0
|
|
O2
|
H:PO41078
|
4.5
|
16.2
|
1.0
|
|
O2B
|
H:ADP1092
|
4.5
|
23.9
|
1.0
|
|
CG
|
H:GLN284
|
4.5
|
12.3
|
1.0
|
|
CD2
|
H:HIS242
|
4.8
|
10.5
|
1.0
|
|
C3'
|
H:ADP1092
|
4.9
|
2.5
|
1.0
|
|
Reference:
J.B.Thoden,
F.M.Raushel,
M.M.Benning,
I.Rayment,
H.M.Holden.
The Structure of Carbamoyl Phosphate Synthetase Determined to 2.1 A Resolution. Acta Crystallogr.,Sect.D V. 55 8 1999.
ISSN: ISSN 0907-4449
PubMed: 10089390
DOI: 10.1107/S0907444998006234
Page generated: Sat Oct 5 11:10:21 2024
|
