Phosphorus in PDB 1ado: Fructose 1,6-Bisphosphate Aldolase From Rabbit Muscle
Enzymatic activity of Fructose 1,6-Bisphosphate Aldolase From Rabbit Muscle
All present enzymatic activity of Fructose 1,6-Bisphosphate Aldolase From Rabbit Muscle:
4.1.2.13;
Protein crystallography data
The structure of Fructose 1,6-Bisphosphate Aldolase From Rabbit Muscle, PDB code: 1ado
was solved by
N.S.Blom,
J.Sygusch,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
12.00 /
1.90
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
163.880,
57.470,
85.030,
90.00,
102.70,
90.00
|
R / Rfree (%)
|
16.2 /
20.3
|
Phosphorus Binding Sites:
The binding sites of Phosphorus atom in the Fructose 1,6-Bisphosphate Aldolase From Rabbit Muscle
(pdb code 1ado). This binding sites where shown within
5.0 Angstroms radius around Phosphorus atom.
In total 3 binding sites of Phosphorus where determined in the
Fructose 1,6-Bisphosphate Aldolase From Rabbit Muscle, PDB code: 1ado:
Jump to Phosphorus binding site number:
1;
2;
3;
Phosphorus binding site 1 out
of 3 in 1ado
Go back to
Phosphorus Binding Sites List in 1ado
Phosphorus binding site 1 out
of 3 in the Fructose 1,6-Bisphosphate Aldolase From Rabbit Muscle
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 1 of Fructose 1,6-Bisphosphate Aldolase From Rabbit Muscle within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:P1104
b:57.9
occ:0.50
|
P
|
A:13P1104
|
0.0
|
57.9
|
0.5
|
P
|
A:13P1104
|
0.3
|
54.8
|
0.5
|
O3P
|
A:13P1104
|
1.4
|
52.4
|
0.5
|
O1P
|
A:13P1104
|
1.5
|
55.1
|
0.5
|
O3P
|
A:13P1104
|
1.6
|
56.8
|
0.5
|
O2P
|
A:13P1104
|
1.6
|
55.2
|
0.5
|
O1P
|
A:13P1104
|
1.6
|
56.0
|
0.5
|
O1
|
A:13P1104
|
1.6
|
55.7
|
0.5
|
O1
|
A:13P1104
|
1.8
|
50.4
|
0.5
|
O2P
|
A:13P1104
|
1.8
|
52.6
|
0.5
|
HOP2
|
A:13P1104
|
2.1
|
56.1
|
0.5
|
HOP2
|
A:13P1104
|
2.3
|
53.9
|
0.5
|
H
|
A:GLY302
|
2.6
|
14.3
|
1.0
|
C1
|
A:13P1104
|
2.7
|
51.5
|
0.5
|
C1
|
A:13P1104
|
2.7
|
45.1
|
0.5
|
H
|
A:SER271
|
3.0
|
17.8
|
1.0
|
N
|
A:GLY302
|
3.4
|
14.0
|
1.0
|
HG
|
A:SER271
|
3.6
|
24.5
|
1.0
|
H
|
A:GLY272
|
3.6
|
25.1
|
1.0
|
C2
|
A:13P1104
|
3.7
|
50.5
|
0.5
|
OG
|
A:SER271
|
3.8
|
28.6
|
1.0
|
HZ3
|
A:LYS229
|
3.8
|
9.2
|
1.0
|
N
|
A:SER271
|
3.9
|
18.5
|
1.0
|
H
|
A:ARG303
|
3.9
|
21.0
|
1.0
|
O
|
A:SER300
|
4.0
|
14.1
|
1.0
|
C2
|
A:13P1104
|
4.0
|
41.7
|
0.5
|
CA
|
A:GLY302
|
4.1
|
15.0
|
1.0
|
O
|
A:HOH1333
|
4.1
|
34.1
|
1.0
|
HO3
|
A:13P1104
|
4.1
|
47.3
|
0.5
|
O2
|
A:13P1104
|
4.1
|
51.0
|
0.5
|
CB
|
A:LEU270
|
4.2
|
15.3
|
1.0
|
C
|
A:TYR301
|
4.3
|
13.4
|
1.0
|
CA
|
A:LEU270
|
4.3
|
16.3
|
1.0
|
CA
|
A:TYR301
|
4.4
|
12.0
|
1.0
|
C3
|
A:13P1104
|
4.4
|
40.6
|
0.5
|
O
|
A:HOH1579
|
4.5
|
42.2
|
1.0
|
O3
|
A:13P1104
|
4.5
|
47.9
|
0.5
|
N
|
A:GLY272
|
4.6
|
24.8
|
1.0
|
C
|
A:LEU270
|
4.6
|
17.3
|
1.0
|
N
|
A:ARG303
|
4.8
|
20.4
|
1.0
|
C3
|
A:13P1104
|
4.8
|
49.0
|
0.5
|
CA
|
A:SER271
|
4.8
|
23.0
|
1.0
|
NZ
|
A:LYS229
|
4.8
|
10.0
|
1.0
|
CB
|
A:SER271
|
4.8
|
23.7
|
1.0
|
C
|
A:SER300
|
5.0
|
12.6
|
1.0
|
C
|
A:GLY302
|
5.0
|
15.2
|
1.0
|
CE
|
A:LYS229
|
5.0
|
9.4
|
1.0
|
|
Phosphorus binding site 2 out
of 3 in 1ado
Go back to
Phosphorus Binding Sites List in 1ado
Phosphorus binding site 2 out
of 3 in the Fructose 1,6-Bisphosphate Aldolase From Rabbit Muscle
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 2 of Fructose 1,6-Bisphosphate Aldolase From Rabbit Muscle within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:P1104
b:54.8
occ:0.50
|
P
|
A:13P1104
|
0.0
|
54.8
|
0.5
|
P
|
A:13P1104
|
0.3
|
57.9
|
0.5
|
O3P
|
A:13P1104
|
1.4
|
56.8
|
0.5
|
O3P
|
A:13P1104
|
1.6
|
52.4
|
0.5
|
O1P
|
A:13P1104
|
1.6
|
56.0
|
0.5
|
O2P
|
A:13P1104
|
1.6
|
52.6
|
0.5
|
O1P
|
A:13P1104
|
1.6
|
55.1
|
0.5
|
O1
|
A:13P1104
|
1.6
|
50.4
|
0.5
|
O2P
|
A:13P1104
|
1.8
|
55.2
|
0.5
|
O1
|
A:13P1104
|
1.8
|
55.7
|
0.5
|
HOP2
|
A:13P1104
|
2.1
|
53.9
|
0.5
|
HOP2
|
A:13P1104
|
2.2
|
56.1
|
0.5
|
C1
|
A:13P1104
|
2.7
|
45.1
|
0.5
|
C1
|
A:13P1104
|
2.8
|
51.5
|
0.5
|
H
|
A:GLY302
|
2.9
|
14.3
|
1.0
|
H
|
A:SER271
|
3.2
|
17.8
|
1.0
|
H
|
A:GLY272
|
3.6
|
25.1
|
1.0
|
N
|
A:GLY302
|
3.7
|
14.0
|
1.0
|
C2
|
A:13P1104
|
3.7
|
50.5
|
0.5
|
HG
|
A:SER271
|
3.8
|
24.5
|
1.0
|
HZ3
|
A:LYS229
|
3.8
|
9.2
|
1.0
|
O
|
A:HOH1333
|
3.8
|
34.1
|
1.0
|
C2
|
A:13P1104
|
3.9
|
41.7
|
0.5
|
OG
|
A:SER271
|
4.0
|
28.6
|
1.0
|
HO3
|
A:13P1104
|
4.0
|
47.3
|
0.5
|
N
|
A:SER271
|
4.0
|
18.5
|
1.0
|
CB
|
A:LEU270
|
4.1
|
15.3
|
1.0
|
O
|
A:SER300
|
4.1
|
14.1
|
1.0
|
H
|
A:ARG303
|
4.1
|
21.0
|
1.0
|
C3
|
A:13P1104
|
4.2
|
40.6
|
0.5
|
O2
|
A:13P1104
|
4.2
|
51.0
|
0.5
|
CA
|
A:GLY302
|
4.3
|
15.0
|
1.0
|
CA
|
A:LEU270
|
4.3
|
16.3
|
1.0
|
O
|
A:HOH1579
|
4.4
|
42.2
|
1.0
|
O3
|
A:13P1104
|
4.5
|
47.9
|
0.5
|
C
|
A:TYR301
|
4.5
|
13.4
|
1.0
|
N
|
A:GLY272
|
4.6
|
24.8
|
1.0
|
CA
|
A:TYR301
|
4.6
|
12.0
|
1.0
|
C
|
A:LEU270
|
4.6
|
17.3
|
1.0
|
NZ
|
A:LYS229
|
4.7
|
10.0
|
1.0
|
C3
|
A:13P1104
|
4.8
|
49.0
|
0.5
|
CE
|
A:LYS229
|
4.9
|
9.4
|
1.0
|
O3
|
A:13P1104
|
4.9
|
38.1
|
0.5
|
HO3
|
A:13P1104
|
4.9
|
39.5
|
0.5
|
CA
|
A:SER271
|
4.9
|
23.0
|
1.0
|
O2
|
A:13P1104
|
5.0
|
38.5
|
0.5
|
N
|
A:ARG303
|
5.0
|
20.4
|
1.0
|
|
Phosphorus binding site 3 out
of 3 in 1ado
Go back to
Phosphorus Binding Sites List in 1ado
Phosphorus binding site 3 out
of 3 in the Fructose 1,6-Bisphosphate Aldolase From Rabbit Muscle
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 3 of Fructose 1,6-Bisphosphate Aldolase From Rabbit Muscle within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:P1053
b:41.6
occ:0.70
|
P
|
B:13P1053
|
0.0
|
41.6
|
0.7
|
O3P
|
B:13P1053
|
1.6
|
42.1
|
0.7
|
O2P
|
B:13P1053
|
1.6
|
40.2
|
0.7
|
O1P
|
B:13P1053
|
1.6
|
41.0
|
0.7
|
O1
|
B:13P1053
|
1.6
|
40.8
|
0.7
|
HOP2
|
B:13P1053
|
2.1
|
40.6
|
0.7
|
C1
|
B:13P1053
|
2.6
|
39.2
|
0.7
|
H
|
B:GLY302
|
2.9
|
16.0
|
1.0
|
H
|
B:SER271
|
3.0
|
18.2
|
1.0
|
H
|
B:GLY272
|
3.2
|
23.7
|
1.0
|
O
|
B:HOH1155
|
3.3
|
34.1
|
1.0
|
OG
|
B:SER271
|
3.4
|
25.1
|
1.0
|
H
|
B:ARG303
|
3.4
|
21.9
|
1.0
|
C2
|
B:13P1053
|
3.5
|
41.8
|
0.7
|
C3
|
B:13P1053
|
3.7
|
43.4
|
0.7
|
HG
|
B:SER271
|
3.7
|
23.6
|
1.0
|
N
|
B:SER271
|
3.8
|
19.2
|
1.0
|
N
|
B:GLY302
|
3.8
|
15.4
|
1.0
|
O
|
B:HOH1198
|
3.9
|
24.8
|
1.0
|
N
|
B:GLY272
|
4.0
|
23.5
|
1.0
|
CA
|
B:GLY302
|
4.2
|
17.1
|
1.0
|
N
|
B:ARG303
|
4.3
|
21.8
|
1.0
|
CB
|
B:LEU270
|
4.4
|
13.8
|
1.0
|
CB
|
B:SER271
|
4.5
|
22.4
|
1.0
|
CA
|
B:SER271
|
4.5
|
21.8
|
1.0
|
H
|
B:GLY273
|
4.5
|
23.4
|
1.0
|
O2
|
B:13P1053
|
4.5
|
41.9
|
0.7
|
C
|
B:LEU270
|
4.6
|
15.4
|
1.0
|
CA
|
B:LEU270
|
4.7
|
15.4
|
1.0
|
O
|
B:HOH1533
|
4.7
|
32.3
|
1.0
|
H
|
B:ALA304
|
4.7
|
23.7
|
1.0
|
C
|
B:SER271
|
4.8
|
23.9
|
1.0
|
C
|
B:GLY302
|
4.8
|
17.6
|
1.0
|
C
|
B:TYR301
|
4.8
|
11.7
|
1.0
|
O
|
B:SER300
|
4.9
|
10.3
|
1.0
|
CA
|
B:GLY272
|
4.9
|
24.4
|
1.0
|
O3
|
B:13P1053
|
5.0
|
43.9
|
0.7
|
|
Reference:
N.Blom,
J.Sygusch.
Product Binding and Role of the C-Terminal Region in Class I D-Fructose 1,6-Bisphosphate Aldolase. Nat.Struct.Biol. V. 4 36 1997.
ISSN: ISSN 1072-8368
PubMed: 8989320
DOI: 10.1038/NSB0197-36
Page generated: Fri Sep 25 12:46:11 2020
|