Potassium in PDB 1bxr: Structure of Carbamoyl Phosphate Synthetase Complexed with the Atp Analog Amppnp
Enzymatic activity of Structure of Carbamoyl Phosphate Synthetase Complexed with the Atp Analog Amppnp
All present enzymatic activity of Structure of Carbamoyl Phosphate Synthetase Complexed with the Atp Analog Amppnp:
6.3.5.5;
Protein crystallography data
The structure of Structure of Carbamoyl Phosphate Synthetase Complexed with the Atp Analog Amppnp, PDB code: 1bxr
was solved by
J.B.Thoden,
G.Wesenberg,
F.M.Raushel,
H.M.Holden,
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 (°)
|
151.900,
164.500,
332.600,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
19.5 /
n/a
|
Other elements in 1bxr:
The structure of Structure of Carbamoyl Phosphate Synthetase Complexed with the Atp Analog Amppnp also contains other interesting chemical elements:
Potassium Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
19;
Binding sites:
The binding sites of Potassium atom in the Structure of Carbamoyl Phosphate Synthetase Complexed with the Atp Analog Amppnp
(pdb code 1bxr). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 19 binding sites of Potassium where determined in the
Structure of Carbamoyl Phosphate Synthetase Complexed with the Atp Analog Amppnp, PDB code: 1bxr:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Potassium binding site 1 out
of 19 in 1bxr
Go back to
Potassium Binding Sites List in 1bxr
Potassium binding site 1 out
of 19 in the Structure of Carbamoyl Phosphate Synthetase Complexed with the Atp Analog Amppnp
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of Structure of Carbamoyl Phosphate Synthetase Complexed with the Atp Analog Amppnp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K1075
b:27.2
occ:1.00
|
O
|
A:ILE242
|
2.6
|
28.9
|
1.0
|
OD1
|
A:ASN236
|
2.6
|
23.7
|
1.0
|
OG
|
A:SER247
|
2.8
|
26.6
|
1.0
|
OE1
|
A:GLU215
|
2.8
|
23.4
|
1.0
|
O
|
A:ASP238
|
2.9
|
20.9
|
1.0
|
O
|
A:ALA239
|
3.1
|
41.0
|
1.0
|
CG
|
A:ASN236
|
3.6
|
22.6
|
1.0
|
C
|
A:ASP238
|
3.7
|
29.0
|
1.0
|
C
|
A:ALA239
|
3.7
|
47.2
|
1.0
|
CB
|
A:SER247
|
3.7
|
17.7
|
1.0
|
CD
|
A:GLU215
|
3.8
|
42.2
|
1.0
|
C
|
A:ILE242
|
3.8
|
33.5
|
1.0
|
CB
|
A:ASN236
|
3.8
|
8.4
|
1.0
|
CB
|
A:GLU215
|
4.2
|
27.0
|
1.0
|
O2'
|
A:ANP1083
|
4.3
|
32.0
|
1.0
|
CG
|
A:GLU215
|
4.3
|
26.1
|
1.0
|
O
|
A:HIS243
|
4.3
|
35.4
|
1.0
|
N
|
A:ALA239
|
4.3
|
25.8
|
1.0
|
CB
|
A:ILE242
|
4.4
|
21.1
|
1.0
|
N
|
A:MET240
|
4.4
|
23.7
|
1.0
|
N
|
A:THR244
|
4.4
|
18.3
|
1.0
|
CB
|
A:ASP238
|
4.4
|
18.0
|
1.0
|
C
|
A:HIS243
|
4.4
|
22.6
|
1.0
|
CA
|
A:ALA239
|
4.4
|
28.5
|
1.0
|
CA
|
A:THR244
|
4.4
|
18.2
|
1.0
|
CA
|
A:ILE242
|
4.5
|
25.3
|
1.0
|
N
|
A:ILE242
|
4.5
|
32.3
|
1.0
|
CG2
|
A:THR244
|
4.5
|
39.3
|
1.0
|
OE2
|
A:GLU215
|
4.5
|
42.1
|
1.0
|
CA
|
A:ASP238
|
4.6
|
27.8
|
1.0
|
CA
|
A:MET240
|
4.6
|
22.9
|
1.0
|
CG2
|
A:ILE242
|
4.8
|
14.9
|
1.0
|
ND2
|
A:ASN236
|
4.8
|
19.7
|
1.0
|
N
|
A:HIS243
|
4.8
|
22.1
|
1.0
|
|
Potassium binding site 2 out
of 19 in 1bxr
Go back to
Potassium Binding Sites List in 1bxr
Potassium binding site 2 out
of 19 in the Structure of Carbamoyl Phosphate Synthetase Complexed with the Atp Analog Amppnp
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of Structure of Carbamoyl Phosphate Synthetase Complexed with the Atp Analog Amppnp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K1076
b:29.0
occ:1.00
|
O
|
A:MET300
|
2.2
|
30.1
|
1.0
|
O
|
A:HOH1199
|
2.5
|
44.8
|
1.0
|
O
|
A:HOH1200
|
2.6
|
59.1
|
1.0
|
OE2
|
A:GLU127
|
3.2
|
48.1
|
1.0
|
O
|
A:HOH1393
|
3.3
|
38.4
|
1.0
|
C
|
A:MET300
|
3.3
|
26.5
|
1.0
|
OE1
|
A:GLU299
|
3.4
|
44.1
|
1.0
|
O
|
A:ALA126
|
3.5
|
42.4
|
1.0
|
OD1
|
A:ASN301
|
3.6
|
35.6
|
1.0
|
CD
|
A:GLU127
|
3.6
|
43.8
|
1.0
|
MN
|
A:MN1074
|
3.8
|
24.3
|
1.0
|
CD
|
A:GLU299
|
3.9
|
37.0
|
1.0
|
C
|
A:ALA126
|
4.0
|
38.7
|
1.0
|
OE1
|
A:GLU127
|
4.0
|
0.0
|
1.0
|
N
|
A:MET300
|
4.0
|
52.9
|
1.0
|
N
|
A:ASN301
|
4.3
|
27.5
|
1.0
|
CA
|
A:MET300
|
4.3
|
24.1
|
1.0
|
NH1
|
A:ARG129
|
4.3
|
48.2
|
1.0
|
CA
|
A:GLU127
|
4.3
|
47.9
|
1.0
|
CA
|
A:ASN301
|
4.3
|
33.9
|
1.0
|
N
|
A:GLU127
|
4.4
|
50.1
|
1.0
|
OE2
|
A:GLU299
|
4.4
|
44.1
|
1.0
|
CG
|
A:ASN301
|
4.5
|
42.2
|
1.0
|
CB
|
A:GLU299
|
4.5
|
25.0
|
1.0
|
CD
|
A:PRO302
|
4.5
|
53.0
|
1.0
|
CB
|
A:ALA126
|
4.5
|
32.4
|
1.0
|
CG
|
A:GLU127
|
4.5
|
23.8
|
1.0
|
CZ
|
A:ARG129
|
4.6
|
47.8
|
1.0
|
CG
|
A:GLU299
|
4.7
|
41.0
|
1.0
|
NH2
|
A:ARG129
|
4.7
|
37.7
|
1.0
|
CA
|
A:ALA126
|
4.8
|
50.6
|
1.0
|
|
Potassium binding site 3 out
of 19 in 1bxr
Go back to
Potassium Binding Sites List in 1bxr
Potassium binding site 3 out
of 19 in the Structure of Carbamoyl Phosphate Synthetase Complexed with the Atp Analog Amppnp
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of Structure of Carbamoyl Phosphate Synthetase Complexed with the Atp Analog Amppnp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K1079
b:26.2
occ:1.00
|
O
|
A:VAL787
|
2.5
|
23.8
|
1.0
|
OG
|
A:SER792
|
2.6
|
22.2
|
1.0
|
OE1
|
A:GLU761
|
2.7
|
26.9
|
1.0
|
ND1
|
A:HIS781
|
2.8
|
24.2
|
1.0
|
O
|
A:GLN784
|
2.9
|
23.2
|
1.0
|
O
|
A:GLU783
|
2.9
|
28.7
|
1.0
|
C
|
A:GLN784
|
3.5
|
25.1
|
1.0
|
CB
|
A:GLU761
|
3.6
|
29.9
|
1.0
|
CB
|
A:SER792
|
3.6
|
15.4
|
1.0
|
C
|
A:VAL787
|
3.7
|
20.8
|
1.0
|
C
|
A:GLU783
|
3.7
|
23.6
|
1.0
|
CD
|
A:GLU761
|
3.7
|
32.7
|
1.0
|
CE1
|
A:HIS781
|
3.7
|
17.4
|
1.0
|
CG
|
A:HIS781
|
3.7
|
24.5
|
1.0
|
CB
|
A:HIS781
|
3.9
|
45.9
|
1.0
|
N
|
A:ALA785
|
4.1
|
23.0
|
1.0
|
CB
|
A:VAL787
|
4.1
|
27.3
|
1.0
|
CG
|
A:GLU761
|
4.2
|
36.4
|
1.0
|
N
|
A:VAL787
|
4.2
|
23.6
|
1.0
|
CA
|
A:ALA785
|
4.2
|
23.9
|
1.0
|
CA
|
A:VAL787
|
4.2
|
17.7
|
1.0
|
N
|
A:GLN784
|
4.3
|
29.7
|
1.0
|
CB
|
A:GLU783
|
4.3
|
16.7
|
1.0
|
CA
|
A:GLN784
|
4.3
|
35.0
|
1.0
|
O2'
|
A:ANP1084
|
4.4
|
21.2
|
1.0
|
C
|
A:HIS788
|
4.5
|
21.0
|
1.0
|
O
|
A:HIS788
|
4.5
|
27.6
|
1.0
|
N
|
A:SER789
|
4.5
|
22.1
|
1.0
|
CA
|
A:GLU783
|
4.5
|
17.7
|
1.0
|
OE2
|
A:GLU761
|
4.5
|
29.5
|
1.0
|
O
|
A:HOH1313
|
4.5
|
21.5
|
1.0
|
CA
|
A:SER789
|
4.7
|
17.7
|
1.0
|
CG1
|
A:VAL787
|
4.7
|
12.1
|
1.0
|
N
|
A:HIS788
|
4.8
|
20.9
|
1.0
|
N
|
A:GLY786
|
4.8
|
32.3
|
1.0
|
C
|
A:ALA785
|
4.9
|
28.1
|
1.0
|
NE2
|
A:HIS781
|
4.9
|
21.0
|
1.0
|
CD2
|
A:HIS781
|
4.9
|
26.5
|
1.0
|
CA
|
A:GLU761
|
4.9
|
24.7
|
1.0
|
CA
|
A:SER792
|
4.9
|
25.1
|
1.0
|
N
|
A:GLU783
|
5.0
|
24.6
|
1.0
|
|
Potassium binding site 4 out
of 19 in 1bxr
Go back to
Potassium Binding Sites List in 1bxr
Potassium binding site 4 out
of 19 in the Structure of Carbamoyl Phosphate Synthetase Complexed with the Atp Analog Amppnp
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 4 of Structure of Carbamoyl Phosphate Synthetase Complexed with the Atp Analog Amppnp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K984
b:31.6
occ:1.00
|
O
|
B:ASP112
|
2.6
|
21.8
|
1.0
|
O
|
B:HIS16
|
2.8
|
31.3
|
1.0
|
O
|
B:HOH1063
|
2.8
|
45.2
|
1.0
|
O
|
B:HOH1009
|
2.9
|
43.4
|
1.0
|
O
|
B:HOH1010
|
3.1
|
31.6
|
1.0
|
C
|
B:ASP112
|
3.8
|
25.5
|
1.0
|
O
|
A:HOH1283
|
3.8
|
53.7
|
1.0
|
C
|
B:HIS16
|
4.0
|
39.0
|
1.0
|
O
|
A:HOH1496
|
4.0
|
38.4
|
1.0
|
O
|
B:HOH1055
|
4.1
|
51.6
|
1.0
|
CA
|
B:ILE113
|
4.2
|
24.6
|
1.0
|
CL
|
B:CL982
|
4.3
|
30.2
|
1.0
|
NH2
|
A:ARG494
|
4.3
|
67.6
|
1.0
|
O
|
A:HOH1597
|
4.3
|
58.4
|
1.0
|
CA
|
B:GLY17
|
4.4
|
22.1
|
1.0
|
N
|
B:ILE113
|
4.5
|
18.1
|
1.0
|
O
|
B:HOH1008
|
4.6
|
37.9
|
1.0
|
CB
|
B:ASP112
|
4.6
|
25.1
|
1.0
|
CG2
|
B:ILE113
|
4.7
|
16.7
|
1.0
|
N
|
B:GLY17
|
4.7
|
26.0
|
1.0
|
CZ
|
A:ARG494
|
4.7
|
38.8
|
1.0
|
NH1
|
A:ARG494
|
4.8
|
30.7
|
1.0
|
CA
|
B:ASP112
|
4.8
|
19.9
|
1.0
|
CB
|
B:ILE113
|
4.9
|
32.2
|
1.0
|
|
Potassium binding site 5 out
of 19 in 1bxr
Go back to
Potassium Binding Sites List in 1bxr
Potassium binding site 5 out
of 19 in the Structure of Carbamoyl Phosphate Synthetase Complexed with the Atp Analog Amppnp
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 5 of Structure of Carbamoyl Phosphate Synthetase Complexed with the Atp Analog Amppnp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K1903
b:19.1
occ:1.00
|
O
|
C:ASP238
|
2.5
|
27.9
|
1.0
|
OE1
|
C:GLU215
|
2.6
|
26.2
|
1.0
|
O
|
C:ILE242
|
2.6
|
26.1
|
1.0
|
O
|
C:ALA239
|
2.7
|
17.6
|
1.0
|
OG
|
C:SER247
|
2.7
|
15.8
|
1.0
|
OD1
|
C:ASN236
|
3.0
|
32.8
|
1.0
|
C
|
C:ASP238
|
3.4
|
18.9
|
1.0
|
C
|
C:ALA239
|
3.5
|
25.9
|
1.0
|
C
|
C:ILE242
|
3.7
|
22.3
|
1.0
|
CD
|
C:GLU215
|
3.8
|
16.8
|
1.0
|
CG
|
C:ASN236
|
3.8
|
12.8
|
1.0
|
CB
|
C:SER247
|
3.8
|
7.6
|
1.0
|
CB
|
C:ASN236
|
3.8
|
15.6
|
1.0
|
N
|
C:ALA239
|
4.2
|
14.6
|
1.0
|
CB
|
C:GLU215
|
4.2
|
11.9
|
1.0
|
N
|
C:ILE242
|
4.2
|
24.7
|
1.0
|
O2'
|
C:ANP1900
|
4.3
|
23.3
|
1.0
|
CA
|
C:ALA239
|
4.3
|
11.0
|
1.0
|
CB
|
C:ASP238
|
4.3
|
18.5
|
1.0
|
CA
|
C:ILE242
|
4.3
|
18.6
|
1.0
|
N
|
C:MET240
|
4.3
|
19.4
|
1.0
|
CB
|
C:ILE242
|
4.3
|
14.5
|
1.0
|
CA
|
C:ASP238
|
4.4
|
14.8
|
1.0
|
CG
|
C:GLU215
|
4.4
|
36.6
|
1.0
|
C
|
C:HIS243
|
4.5
|
12.2
|
1.0
|
O
|
C:HIS243
|
4.5
|
33.2
|
1.0
|
N
|
C:THR244
|
4.5
|
26.0
|
1.0
|
CA
|
C:MET240
|
4.5
|
13.4
|
1.0
|
OE2
|
C:GLU215
|
4.6
|
31.8
|
1.0
|
CA
|
C:THR244
|
4.6
|
16.9
|
1.0
|
N
|
C:HIS243
|
4.8
|
17.2
|
1.0
|
CG2
|
C:THR244
|
4.9
|
6.3
|
1.0
|
N
|
C:GLY241
|
4.9
|
14.3
|
1.0
|
CG2
|
C:ILE242
|
4.9
|
16.6
|
1.0
|
C
|
C:MET240
|
5.0
|
31.7
|
1.0
|
N
|
C:ASP238
|
5.0
|
17.3
|
1.0
|
|
Potassium binding site 6 out
of 19 in 1bxr
Go back to
Potassium Binding Sites List in 1bxr
Potassium binding site 6 out
of 19 in the Structure of Carbamoyl Phosphate Synthetase Complexed with the Atp Analog Amppnp
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 6 of Structure of Carbamoyl Phosphate Synthetase Complexed with the Atp Analog Amppnp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K1904
b:31.7
occ:1.00
|
O
|
C:MET300
|
2.8
|
26.0
|
1.0
|
O
|
C:HOH4100
|
2.8
|
24.0
|
1.0
|
OE2
|
C:GLU127
|
2.8
|
38.7
|
1.0
|
O
|
C:HOH4101
|
2.9
|
26.1
|
1.0
|
OE1
|
C:GLU299
|
2.9
|
28.8
|
1.0
|
O
|
C:ALA126
|
3.1
|
27.3
|
1.0
|
O
|
C:HOH4295
|
3.4
|
33.6
|
1.0
|
CD
|
C:GLU127
|
3.6
|
46.1
|
1.0
|
OD1
|
C:ASN301
|
3.8
|
29.1
|
1.0
|
MN
|
C:MN1901
|
3.8
|
29.0
|
1.0
|
C
|
C:MET300
|
3.8
|
20.6
|
1.0
|
CD
|
C:GLU299
|
3.9
|
22.0
|
1.0
|
C
|
C:ALA126
|
3.9
|
24.4
|
1.0
|
OE1
|
C:GLU127
|
4.0
|
59.7
|
1.0
|
NH1
|
C:ARG129
|
4.1
|
30.7
|
1.0
|
CA
|
C:GLU127
|
4.2
|
14.0
|
1.0
|
N
|
C:MET300
|
4.4
|
21.7
|
1.0
|
N
|
C:GLU127
|
4.4
|
25.1
|
1.0
|
CB
|
C:GLU299
|
4.4
|
21.0
|
1.0
|
CA
|
C:ASN301
|
4.4
|
23.0
|
1.0
|
N
|
C:ASN301
|
4.5
|
20.4
|
1.0
|
CZ
|
C:ARG129
|
4.5
|
24.1
|
1.0
|
CG
|
C:ASN301
|
4.6
|
21.8
|
1.0
|
NH2
|
C:ARG129
|
4.6
|
17.9
|
1.0
|
CD
|
C:PRO302
|
4.7
|
36.4
|
1.0
|
CG
|
C:GLU299
|
4.7
|
10.6
|
1.0
|
CG
|
C:GLU127
|
4.7
|
21.0
|
1.0
|
CB
|
C:ALA126
|
4.8
|
19.9
|
1.0
|
OE2
|
C:GLU299
|
4.8
|
28.9
|
1.0
|
CA
|
C:MET300
|
4.8
|
8.9
|
1.0
|
O
|
C:GLU127
|
4.9
|
28.9
|
1.0
|
C
|
C:GLU127
|
4.9
|
23.4
|
1.0
|
O2B
|
C:ANP1900
|
4.9
|
28.3
|
1.0
|
CA
|
C:ALA126
|
4.9
|
20.1
|
1.0
|
O
|
C:HOH4294
|
5.0
|
19.1
|
1.0
|
|
Potassium binding site 7 out
of 19 in 1bxr
Go back to
Potassium Binding Sites List in 1bxr
Potassium binding site 7 out
of 19 in the Structure of Carbamoyl Phosphate Synthetase Complexed with the Atp Analog Amppnp
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 7 of Structure of Carbamoyl Phosphate Synthetase Complexed with the Atp Analog Amppnp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K1913
b:30.9
occ:1.00
|
O
|
C:VAL787
|
2.6
|
38.4
|
1.0
|
OG
|
C:SER792
|
2.7
|
20.7
|
1.0
|
OE1
|
C:GLU761
|
2.7
|
40.6
|
1.0
|
O
|
C:GLU783
|
2.8
|
33.8
|
1.0
|
O
|
C:GLN784
|
2.9
|
33.6
|
1.0
|
ND1
|
C:HIS781
|
2.9
|
35.2
|
1.0
|
C
|
C:GLN784
|
3.5
|
32.2
|
1.0
|
CB
|
C:SER792
|
3.6
|
17.4
|
1.0
|
C
|
C:GLU783
|
3.6
|
27.2
|
1.0
|
CG
|
C:HIS781
|
3.8
|
22.6
|
1.0
|
C
|
C:VAL787
|
3.8
|
23.8
|
1.0
|
CB
|
C:GLU761
|
3.8
|
18.0
|
1.0
|
CD
|
C:GLU761
|
3.9
|
53.3
|
1.0
|
CB
|
C:HIS781
|
3.9
|
45.4
|
1.0
|
CE1
|
C:HIS781
|
3.9
|
20.9
|
1.0
|
N
|
C:ALA785
|
4.0
|
26.2
|
1.0
|
CB
|
C:VAL787
|
4.1
|
18.5
|
1.0
|
CA
|
C:ALA785
|
4.2
|
42.4
|
1.0
|
CA
|
C:GLN784
|
4.3
|
30.8
|
1.0
|
N
|
C:GLN784
|
4.3
|
32.3
|
1.0
|
CG
|
C:GLU761
|
4.3
|
42.5
|
1.0
|
CA
|
C:VAL787
|
4.3
|
64.7
|
1.0
|
N
|
C:VAL787
|
4.4
|
36.0
|
1.0
|
CB
|
C:GLU783
|
4.4
|
21.9
|
1.0
|
O2'
|
C:ANP1910
|
4.5
|
36.0
|
1.0
|
CA
|
C:GLU783
|
4.5
|
22.0
|
1.0
|
O
|
C:HIS788
|
4.5
|
33.9
|
1.0
|
C
|
C:HIS788
|
4.6
|
20.9
|
1.0
|
N
|
C:SER789
|
4.6
|
29.9
|
1.0
|
CG1
|
C:VAL787
|
4.6
|
17.1
|
1.0
|
CA
|
C:SER789
|
4.7
|
33.9
|
1.0
|
OE2
|
C:GLU761
|
4.8
|
55.5
|
1.0
|
C
|
C:ALA785
|
4.8
|
44.8
|
1.0
|
O
|
C:HOH4214
|
4.8
|
35.5
|
1.0
|
N
|
C:GLY786
|
4.9
|
31.3
|
1.0
|
N
|
C:HIS788
|
4.9
|
27.4
|
1.0
|
CD2
|
C:HIS781
|
4.9
|
28.4
|
1.0
|
CA
|
C:SER792
|
5.0
|
27.0
|
1.0
|
NE2
|
C:HIS781
|
5.0
|
27.3
|
1.0
|
N
|
C:GLU783
|
5.0
|
25.3
|
1.0
|
|
Potassium binding site 8 out
of 19 in 1bxr
Go back to
Potassium Binding Sites List in 1bxr
Potassium binding site 8 out
of 19 in the Structure of Carbamoyl Phosphate Synthetase Complexed with the Atp Analog Amppnp
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 8 of Structure of Carbamoyl Phosphate Synthetase Complexed with the Atp Analog Amppnp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K3985
b:54.7
occ:1.00
|
O
|
C:HOH4027
|
2.4
|
30.2
|
1.0
|
OG1
|
C:THR143
|
2.8
|
27.6
|
1.0
|
O
|
C:THR143
|
2.9
|
26.2
|
1.0
|
O
|
C:ALA144
|
3.0
|
32.5
|
1.0
|
O
|
C:HOH4026
|
3.2
|
27.7
|
1.0
|
O
|
C:HOH4461
|
3.2
|
59.1
|
1.0
|
O
|
C:HOH4313
|
3.3
|
50.6
|
1.0
|
C
|
C:ALA144
|
3.4
|
39.6
|
1.0
|
C
|
C:THR143
|
3.5
|
19.3
|
1.0
|
N
|
C:ARG145
|
3.8
|
25.2
|
1.0
|
CA
|
C:ARG145
|
4.0
|
36.0
|
1.0
|
CB
|
C:THR143
|
4.0
|
20.9
|
1.0
|
N
|
C:ALA144
|
4.1
|
27.7
|
1.0
|
CA
|
C:THR143
|
4.2
|
13.5
|
1.0
|
CA
|
C:ALA144
|
4.2
|
16.7
|
1.0
|
N
|
C:THR143
|
4.2
|
21.2
|
1.0
|
O
|
C:HOH4462
|
4.4
|
46.5
|
1.0
|
OG
|
C:SER146
|
4.5
|
29.2
|
1.0
|
OD1
|
C:ASP133
|
4.5
|
35.2
|
1.0
|
OD2
|
C:ASP133
|
4.6
|
48.7
|
1.0
|
N
|
C:SER146
|
4.7
|
22.4
|
1.0
|
O
|
C:HOH4460
|
4.8
|
39.0
|
1.0
|
C
|
C:ARG145
|
4.8
|
23.6
|
1.0
|
O
|
C:HOH4463
|
4.8
|
47.9
|
1.0
|
|
Potassium binding site 9 out
of 19 in 1bxr
Go back to
Potassium Binding Sites List in 1bxr
Potassium binding site 9 out
of 19 in the Structure of Carbamoyl Phosphate Synthetase Complexed with the Atp Analog Amppnp
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 9 of Structure of Carbamoyl Phosphate Synthetase Complexed with the Atp Analog Amppnp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:K3984
b:49.7
occ:1.00
|
O
|
D:HOH1529
|
2.6
|
57.6
|
1.0
|
O
|
D:HIS16
|
2.6
|
32.1
|
1.0
|
O
|
C:HOH4183
|
2.7
|
32.5
|
1.0
|
O
|
D:ASP112
|
2.7
|
36.2
|
1.0
|
O
|
D:HOH1219
|
3.1
|
41.6
|
1.0
|
O
|
C:HOH4184
|
3.8
|
33.0
|
1.0
|
C
|
D:HIS16
|
3.8
|
23.9
|
1.0
|
C
|
D:ASP112
|
4.0
|
24.0
|
1.0
|
NH2
|
C:ARG494
|
4.3
|
34.2
|
1.0
|
CL
|
D:CL1982
|
4.3
|
32.1
|
1.0
|
O
|
D:HOH1466
|
4.3
|
64.8
|
1.0
|
O
|
C:HOH4400
|
4.4
|
37.4
|
1.0
|
CA
|
D:ILE113
|
4.4
|
18.6
|
1.0
|
CA
|
D:GLY17
|
4.6
|
17.4
|
1.0
|
CZ
|
C:ARG494
|
4.6
|
27.7
|
1.0
|
O
|
D:HOH1218
|
4.6
|
39.2
|
1.0
|
CB
|
D:ASP112
|
4.6
|
29.7
|
1.0
|
N
|
D:GLY17
|
4.7
|
23.1
|
1.0
|
N
|
D:ILE113
|
4.7
|
32.5
|
1.0
|
NH1
|
C:ARG494
|
4.8
|
24.3
|
1.0
|
CG2
|
D:ILE113
|
4.8
|
17.1
|
1.0
|
CA
|
D:HIS16
|
4.8
|
25.1
|
1.0
|
CA
|
D:ASP112
|
4.9
|
24.2
|
1.0
|
|
Potassium binding site 10 out
of 19 in 1bxr
Go back to
Potassium Binding Sites List in 1bxr
Potassium binding site 10 out
of 19 in the Structure of Carbamoyl Phosphate Synthetase Complexed with the Atp Analog Amppnp
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 10 of Structure of Carbamoyl Phosphate Synthetase Complexed with the Atp Analog Amppnp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:K2903
b:27.1
occ:1.00
|
OE1
|
E:GLU215
|
2.5
|
32.4
|
1.0
|
O
|
E:ILE242
|
2.5
|
31.4
|
1.0
|
OG
|
E:SER247
|
2.6
|
22.5
|
1.0
|
O
|
E:ASP238
|
2.6
|
28.5
|
1.0
|
O
|
E:ALA239
|
2.9
|
32.1
|
1.0
|
OD1
|
E:ASN236
|
2.9
|
32.7
|
1.0
|
C
|
E:ASP238
|
3.6
|
30.1
|
1.0
|
C
|
E:ALA239
|
3.6
|
21.3
|
1.0
|
CB
|
E:SER247
|
3.7
|
10.3
|
1.0
|
C
|
E:ILE242
|
3.7
|
24.5
|
1.0
|
CG
|
E:ASN236
|
3.7
|
22.8
|
1.0
|
CD
|
E:GLU215
|
3.7
|
30.4
|
1.0
|
CB
|
E:ASN236
|
3.9
|
19.0
|
1.0
|
O2'
|
E:ANP2900
|
4.1
|
27.3
|
1.0
|
CB
|
E:ILE242
|
4.1
|
24.8
|
1.0
|
CB
|
E:GLU215
|
4.2
|
15.4
|
1.0
|
O
|
E:HIS243
|
4.3
|
27.5
|
1.0
|
CA
|
E:THR244
|
4.3
|
14.8
|
1.0
|
N
|
E:THR244
|
4.3
|
24.2
|
1.0
|
CA
|
E:ILE242
|
4.3
|
18.2
|
1.0
|
N
|
E:MET240
|
4.3
|
32.0
|
1.0
|
N
|
E:ALA239
|
4.3
|
27.8
|
1.0
|
N
|
E:ILE242
|
4.3
|
29.0
|
1.0
|
CB
|
E:ASP238
|
4.4
|
16.6
|
1.0
|
C
|
E:HIS243
|
4.4
|
19.9
|
1.0
|
CA
|
E:ALA239
|
4.4
|
51.9
|
1.0
|
CG
|
E:GLU215
|
4.4
|
23.9
|
1.0
|
CA
|
E:ASP238
|
4.5
|
25.7
|
1.0
|
CA
|
E:MET240
|
4.5
|
18.4
|
1.0
|
OE2
|
E:GLU215
|
4.6
|
37.0
|
1.0
|
CG2
|
E:THR244
|
4.6
|
25.0
|
1.0
|
CG2
|
E:ILE242
|
4.6
|
14.3
|
1.0
|
N
|
E:HIS243
|
4.8
|
24.2
|
1.0
|
O3'
|
E:ANP2900
|
5.0
|
24.5
|
1.0
|
ND2
|
E:ASN236
|
5.0
|
21.9
|
1.0
|
C
|
E:MET240
|
5.0
|
26.8
|
1.0
|
|
Reference:
J.B.Thoden,
G.Wesenberg,
F.M.Raushel,
H.M.Holden.
Carbamoyl Phosphate Synthetase: Closure of the B-Domain As A Result of Nucleotide Binding. Biochemistry V. 38 2347 1999.
ISSN: ISSN 0006-2960
PubMed: 10029528
DOI: 10.1021/BI982517H
Page generated: Mon Aug 12 04:05:46 2024
|