Phosphorus in PDB 1abb: Control of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies on R-State Glycogen Phosphorylase Reconstituted with Pyridoxal 5'-Diphosphate
Enzymatic activity of Control of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies on R-State Glycogen Phosphorylase Reconstituted with Pyridoxal 5'-Diphosphate
All present enzymatic activity of Control of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies on R-State Glycogen Phosphorylase Reconstituted with Pyridoxal 5'-Diphosphate:
2.4.1.1;
Protein crystallography data
The structure of Control of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies on R-State Glycogen Phosphorylase Reconstituted with Pyridoxal 5'-Diphosphate, PDB code: 1abb
was solved by
D.D.Leonidas,
N.G.Oikonomakos,
A.C.Papageorgiou,
K.R.Acharya,
D.Barford,
L.N.Johnson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
8.00 /
2.80
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
119.000,
188.100,
88.100,
90.00,
109.29,
90.00
|
R / Rfree (%)
|
21 /
n/a
|
Phosphorus Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
12;
Binding sites:
The binding sites of Phosphorus atom in the Control of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies on R-State Glycogen Phosphorylase Reconstituted with Pyridoxal 5'-Diphosphate
(pdb code 1abb). This binding sites where shown within
5.0 Angstroms radius around Phosphorus atom.
In total 12 binding sites of Phosphorus where determined in the
Control of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies on R-State Glycogen Phosphorylase Reconstituted with Pyridoxal 5'-Diphosphate, PDB code: 1abb:
Jump to Phosphorus binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Phosphorus binding site 1 out
of 12 in 1abb
Go back to
Phosphorus Binding Sites List in 1abb
Phosphorus binding site 1 out
of 12 in the Control of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies on R-State Glycogen Phosphorylase Reconstituted with Pyridoxal 5'-Diphosphate
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 1 of Control of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies on R-State Glycogen Phosphorylase Reconstituted with Pyridoxal 5'-Diphosphate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:P931
b:21.1
occ:1.00
|
PA
|
A:PDP931
|
0.0
|
21.1
|
1.0
|
O1A
|
A:PDP931
|
1.5
|
25.9
|
1.0
|
O2A
|
A:PDP931
|
1.5
|
25.9
|
1.0
|
O5A
|
A:PDP931
|
1.6
|
22.2
|
1.0
|
O3A
|
A:PDP931
|
1.7
|
41.5
|
1.0
|
C5A
|
A:PDP931
|
2.8
|
10.0
|
1.0
|
PB
|
A:PDP931
|
2.9
|
65.8
|
1.0
|
NZ
|
A:LYS568
|
3.2
|
26.7
|
1.0
|
O3B
|
A:PDP931
|
3.3
|
65.7
|
1.0
|
O2B
|
A:PDP931
|
3.5
|
62.0
|
1.0
|
C5
|
A:PDP931
|
4.0
|
4.9
|
1.0
|
CE
|
A:LYS568
|
4.0
|
18.0
|
1.0
|
O1B
|
A:PDP931
|
4.1
|
61.3
|
1.0
|
N
|
A:GLY677
|
4.3
|
10.0
|
1.0
|
CD
|
A:LYS568
|
4.3
|
11.9
|
1.0
|
C6
|
A:PDP931
|
4.4
|
3.4
|
1.0
|
N
|
A:THR676
|
4.7
|
16.3
|
1.0
|
CA
|
A:GLY675
|
4.9
|
20.7
|
1.0
|
CA
|
A:GLY677
|
4.9
|
5.4
|
1.0
|
C
|
A:GLY675
|
4.9
|
19.1
|
1.0
|
C4
|
A:PDP931
|
5.0
|
3.1
|
1.0
|
|
Phosphorus binding site 2 out
of 12 in 1abb
Go back to
Phosphorus Binding Sites List in 1abb
Phosphorus binding site 2 out
of 12 in the Control of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies on R-State Glycogen Phosphorylase Reconstituted with Pyridoxal 5'-Diphosphate
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 2 of Control of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies on R-State Glycogen Phosphorylase Reconstituted with Pyridoxal 5'-Diphosphate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:P931
b:65.8
occ:1.00
|
PB
|
A:PDP931
|
0.0
|
65.8
|
1.0
|
O1B
|
A:PDP931
|
1.5
|
61.3
|
1.0
|
O2B
|
A:PDP931
|
1.5
|
62.0
|
1.0
|
O3B
|
A:PDP931
|
1.5
|
65.7
|
1.0
|
O3A
|
A:PDP931
|
1.7
|
41.5
|
1.0
|
PA
|
A:PDP931
|
2.9
|
21.1
|
1.0
|
O2A
|
A:PDP931
|
3.5
|
25.9
|
1.0
|
O5A
|
A:PDP931
|
3.7
|
22.2
|
1.0
|
CE
|
A:LYS574
|
3.9
|
12.7
|
1.0
|
NZ
|
A:LYS574
|
4.0
|
9.9
|
1.0
|
O1A
|
A:PDP931
|
4.0
|
25.9
|
1.0
|
NZ
|
A:LYS568
|
4.0
|
26.7
|
1.0
|
CD
|
A:LYS568
|
4.2
|
11.9
|
1.0
|
CB
|
A:ARG569
|
4.3
|
28.1
|
1.0
|
N
|
A:ARG569
|
4.3
|
18.8
|
1.0
|
CD
|
A:ARG569
|
4.5
|
50.3
|
1.0
|
CE
|
A:LYS568
|
4.7
|
18.0
|
1.0
|
C5A
|
A:PDP931
|
4.8
|
10.0
|
1.0
|
OE2
|
A:GLU672
|
4.8
|
58.7
|
1.0
|
|
Phosphorus binding site 3 out
of 12 in 1abb
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Phosphorus Binding Sites List in 1abb
Phosphorus binding site 3 out
of 12 in the Control of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies on R-State Glycogen Phosphorylase Reconstituted with Pyridoxal 5'-Diphosphate
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 3 of Control of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies on R-State Glycogen Phosphorylase Reconstituted with Pyridoxal 5'-Diphosphate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:P920
b:45.4
occ:1.00
|
P
|
A:IMP920
|
0.0
|
45.4
|
1.0
|
O3P
|
A:IMP920
|
1.4
|
51.7
|
1.0
|
O1P
|
A:IMP920
|
1.5
|
49.0
|
1.0
|
O2P
|
A:IMP920
|
1.5
|
42.6
|
1.0
|
O5'
|
A:IMP920
|
1.7
|
40.9
|
1.0
|
C5'
|
A:IMP920
|
2.8
|
34.6
|
1.0
|
NH2
|
A:ARG310
|
3.2
|
10.8
|
1.0
|
NH2
|
A:ARG309
|
3.4
|
44.2
|
1.0
|
NE
|
A:ARG310
|
3.5
|
4.6
|
1.0
|
OH
|
A:TYR75
|
3.7
|
79.6
|
1.0
|
CZ
|
A:ARG310
|
3.8
|
10.6
|
1.0
|
C4'
|
A:IMP920
|
4.2
|
32.8
|
1.0
|
CE1
|
A:TYR75
|
4.3
|
79.2
|
1.0
|
O4'
|
A:IMP920
|
4.3
|
33.7
|
1.0
|
CZ
|
A:TYR75
|
4.4
|
80.8
|
1.0
|
CG
|
A:ARG310
|
4.6
|
21.5
|
1.0
|
CZ
|
A:ARG309
|
4.7
|
42.6
|
1.0
|
CD
|
A:ARG310
|
4.7
|
6.8
|
1.0
|
C3'
|
A:IMP920
|
4.9
|
35.0
|
1.0
|
C8
|
A:IMP920
|
5.0
|
44.4
|
1.0
|
|
Phosphorus binding site 4 out
of 12 in 1abb
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Phosphorus Binding Sites List in 1abb
Phosphorus binding site 4 out
of 12 in the Control of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies on R-State Glycogen Phosphorylase Reconstituted with Pyridoxal 5'-Diphosphate
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 4 of Control of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies on R-State Glycogen Phosphorylase Reconstituted with Pyridoxal 5'-Diphosphate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:P932
b:23.8
occ:1.00
|
PA
|
B:PDP932
|
0.0
|
23.8
|
1.0
|
O1A
|
B:PDP932
|
1.5
|
17.6
|
1.0
|
O2A
|
B:PDP932
|
1.5
|
24.4
|
1.0
|
O3A
|
B:PDP932
|
1.6
|
37.9
|
1.0
|
O5A
|
B:PDP932
|
1.6
|
26.0
|
1.0
|
C5A
|
B:PDP932
|
2.7
|
22.1
|
1.0
|
PB
|
B:PDP932
|
2.8
|
59.2
|
1.0
|
O3B
|
B:PDP932
|
3.2
|
67.7
|
1.0
|
O2B
|
B:PDP932
|
3.3
|
60.2
|
1.0
|
NZ
|
B:LYS568
|
3.3
|
18.8
|
1.0
|
N
|
B:GLY677
|
3.9
|
6.4
|
1.0
|
O1B
|
B:PDP932
|
4.0
|
61.7
|
1.0
|
C5
|
B:PDP932
|
4.0
|
14.5
|
1.0
|
N
|
B:THR676
|
4.2
|
23.0
|
1.0
|
CE
|
B:LYS568
|
4.3
|
13.3
|
1.0
|
C6
|
B:PDP932
|
4.6
|
15.4
|
1.0
|
CA
|
B:GLY675
|
4.6
|
19.0
|
1.0
|
CA
|
B:GLY677
|
4.7
|
3.6
|
1.0
|
C
|
B:GLY675
|
4.7
|
21.1
|
1.0
|
CD
|
B:LYS568
|
4.8
|
9.9
|
1.0
|
C
|
B:THR676
|
4.8
|
6.5
|
1.0
|
C4
|
B:PDP932
|
4.9
|
9.5
|
1.0
|
CA
|
B:THR676
|
5.0
|
13.2
|
1.0
|
C4A
|
B:PDP932
|
5.0
|
11.1
|
1.0
|
|
Phosphorus binding site 5 out
of 12 in 1abb
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Phosphorus Binding Sites List in 1abb
Phosphorus binding site 5 out
of 12 in the Control of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies on R-State Glycogen Phosphorylase Reconstituted with Pyridoxal 5'-Diphosphate
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 5 of Control of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies on R-State Glycogen Phosphorylase Reconstituted with Pyridoxal 5'-Diphosphate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:P932
b:59.2
occ:1.00
|
PB
|
B:PDP932
|
0.0
|
59.2
|
1.0
|
O2B
|
B:PDP932
|
1.5
|
60.2
|
1.0
|
O3B
|
B:PDP932
|
1.5
|
67.7
|
1.0
|
O1B
|
B:PDP932
|
1.5
|
61.7
|
1.0
|
O3A
|
B:PDP932
|
1.6
|
37.9
|
1.0
|
PA
|
B:PDP932
|
2.8
|
23.8
|
1.0
|
O5A
|
B:PDP932
|
3.2
|
26.0
|
1.0
|
O2A
|
B:PDP932
|
3.6
|
24.4
|
1.0
|
NE
|
B:ARG569
|
3.8
|
60.5
|
1.0
|
NH2
|
B:ARG569
|
3.9
|
71.6
|
1.0
|
O1A
|
B:PDP932
|
3.9
|
17.6
|
1.0
|
NZ
|
B:LYS568
|
3.9
|
18.8
|
1.0
|
CZ
|
B:ARG569
|
3.9
|
66.7
|
1.0
|
NZ
|
B:LYS574
|
4.0
|
19.6
|
1.0
|
N
|
B:ARG569
|
4.2
|
23.8
|
1.0
|
CD
|
B:LYS568
|
4.2
|
9.9
|
1.0
|
CE
|
B:LYS574
|
4.4
|
8.1
|
1.0
|
CB
|
B:ARG569
|
4.5
|
33.7
|
1.0
|
C5A
|
B:PDP932
|
4.5
|
22.1
|
1.0
|
CA
|
B:LYS568
|
4.5
|
17.6
|
1.0
|
CE
|
B:LYS568
|
4.6
|
13.3
|
1.0
|
CD
|
B:ARG569
|
4.6
|
52.5
|
1.0
|
CG
|
B:LYS568
|
4.7
|
3.0
|
1.0
|
CB
|
B:LYS568
|
4.7
|
9.6
|
1.0
|
NH1
|
B:ARG569
|
4.8
|
68.7
|
1.0
|
CD
|
B:LYS574
|
4.9
|
7.9
|
1.0
|
C
|
B:LYS568
|
4.9
|
22.5
|
1.0
|
CA
|
B:ARG569
|
5.0
|
26.6
|
1.0
|
CG
|
B:ARG569
|
5.0
|
44.1
|
1.0
|
|
Phosphorus binding site 6 out
of 12 in 1abb
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Phosphorus Binding Sites List in 1abb
Phosphorus binding site 6 out
of 12 in the Control of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies on R-State Glycogen Phosphorylase Reconstituted with Pyridoxal 5'-Diphosphate
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 6 of Control of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies on R-State Glycogen Phosphorylase Reconstituted with Pyridoxal 5'-Diphosphate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:P920
b:28.2
occ:1.00
|
P
|
B:IMP920
|
0.0
|
28.2
|
1.0
|
O1P
|
B:IMP920
|
1.5
|
32.0
|
1.0
|
O3P
|
B:IMP920
|
1.5
|
25.1
|
1.0
|
O2P
|
B:IMP920
|
1.5
|
21.5
|
1.0
|
O5'
|
B:IMP920
|
1.6
|
23.2
|
1.0
|
C5'
|
B:IMP920
|
2.7
|
23.1
|
1.0
|
NH2
|
B:ARG309
|
3.1
|
62.8
|
1.0
|
OH
|
B:TYR75
|
3.2
|
55.1
|
1.0
|
NH2
|
B:ARG310
|
3.4
|
10.8
|
1.0
|
NE
|
B:ARG310
|
3.6
|
9.1
|
1.0
|
CZ
|
B:ARG310
|
4.0
|
8.8
|
1.0
|
CZ
|
B:TYR75
|
4.2
|
56.8
|
1.0
|
C4'
|
B:IMP920
|
4.2
|
18.0
|
1.0
|
O4'
|
B:IMP920
|
4.3
|
18.9
|
1.0
|
CZ
|
B:ARG309
|
4.4
|
58.7
|
1.0
|
C8
|
B:IMP920
|
4.7
|
23.1
|
1.0
|
CD
|
B:ARG310
|
4.7
|
11.1
|
1.0
|
CG
|
B:ARG310
|
4.7
|
10.4
|
1.0
|
CE1
|
B:TYR75
|
4.7
|
57.5
|
1.0
|
CE2
|
B:TYR75
|
5.0
|
55.5
|
1.0
|
|
Phosphorus binding site 7 out
of 12 in 1abb
Go back to
Phosphorus Binding Sites List in 1abb
Phosphorus binding site 7 out
of 12 in the Control of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies on R-State Glycogen Phosphorylase Reconstituted with Pyridoxal 5'-Diphosphate
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 7 of Control of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies on R-State Glycogen Phosphorylase Reconstituted with Pyridoxal 5'-Diphosphate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:P933
b:18.5
occ:1.00
|
PA
|
C:PDP933
|
0.0
|
18.5
|
1.0
|
O1A
|
C:PDP933
|
1.5
|
30.6
|
1.0
|
O2A
|
C:PDP933
|
1.5
|
28.7
|
1.0
|
O3A
|
C:PDP933
|
1.6
|
40.1
|
1.0
|
O5A
|
C:PDP933
|
1.6
|
20.8
|
1.0
|
C5A
|
C:PDP933
|
2.7
|
11.9
|
1.0
|
PB
|
C:PDP933
|
2.9
|
66.0
|
1.0
|
O2B
|
C:PDP933
|
3.3
|
62.2
|
1.0
|
O3B
|
C:PDP933
|
3.4
|
66.3
|
1.0
|
NZ
|
C:LYS568
|
3.6
|
36.8
|
1.0
|
N
|
C:GLY677
|
3.7
|
12.8
|
1.0
|
CA
|
C:GLY677
|
3.8
|
10.5
|
1.0
|
O1B
|
C:PDP933
|
4.0
|
67.7
|
1.0
|
C5
|
C:PDP933
|
4.0
|
7.9
|
1.0
|
CE
|
C:LYS568
|
4.4
|
24.4
|
1.0
|
CD
|
C:LYS568
|
4.6
|
23.1
|
1.0
|
C6
|
C:PDP933
|
4.7
|
6.0
|
1.0
|
N
|
C:THR676
|
4.8
|
19.0
|
1.0
|
C4
|
C:PDP933
|
4.8
|
7.2
|
1.0
|
C4A
|
C:PDP933
|
4.8
|
2.0
|
1.0
|
C
|
C:THR676
|
4.8
|
15.8
|
1.0
|
O
|
C:VAL567
|
4.9
|
29.7
|
1.0
|
|
Phosphorus binding site 8 out
of 12 in 1abb
Go back to
Phosphorus Binding Sites List in 1abb
Phosphorus binding site 8 out
of 12 in the Control of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies on R-State Glycogen Phosphorylase Reconstituted with Pyridoxal 5'-Diphosphate
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 8 of Control of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies on R-State Glycogen Phosphorylase Reconstituted with Pyridoxal 5'-Diphosphate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:P933
b:66.0
occ:1.00
|
PB
|
C:PDP933
|
0.0
|
66.0
|
1.0
|
O1B
|
C:PDP933
|
1.5
|
67.7
|
1.0
|
O2B
|
C:PDP933
|
1.5
|
62.2
|
1.0
|
O3B
|
C:PDP933
|
1.5
|
66.3
|
1.0
|
O3A
|
C:PDP933
|
1.6
|
40.1
|
1.0
|
PA
|
C:PDP933
|
2.9
|
18.5
|
1.0
|
O5A
|
C:PDP933
|
3.4
|
20.8
|
1.0
|
O1A
|
C:PDP933
|
3.7
|
30.6
|
1.0
|
O2A
|
C:PDP933
|
3.8
|
28.7
|
1.0
|
NZ
|
C:LYS574
|
3.8
|
22.7
|
1.0
|
NZ
|
C:LYS568
|
4.0
|
36.8
|
1.0
|
CE
|
C:LYS574
|
4.2
|
21.5
|
1.0
|
C5A
|
C:PDP933
|
4.3
|
11.9
|
1.0
|
CD
|
C:LYS568
|
4.4
|
23.1
|
1.0
|
CB
|
C:ARG569
|
4.6
|
23.0
|
1.0
|
N
|
C:ARG569
|
4.7
|
14.8
|
1.0
|
CE
|
C:LYS568
|
4.8
|
24.4
|
1.0
|
CD
|
C:ARG569
|
4.9
|
34.6
|
1.0
|
|
Phosphorus binding site 9 out
of 12 in 1abb
Go back to
Phosphorus Binding Sites List in 1abb
Phosphorus binding site 9 out
of 12 in the Control of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies on R-State Glycogen Phosphorylase Reconstituted with Pyridoxal 5'-Diphosphate
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 9 of Control of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies on R-State Glycogen Phosphorylase Reconstituted with Pyridoxal 5'-Diphosphate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:P920
b:26.2
occ:1.00
|
P
|
C:IMP920
|
0.0
|
26.2
|
1.0
|
O3P
|
C:IMP920
|
1.5
|
20.3
|
1.0
|
O1P
|
C:IMP920
|
1.5
|
33.3
|
1.0
|
O2P
|
C:IMP920
|
1.5
|
25.6
|
1.0
|
O5'
|
C:IMP920
|
1.6
|
18.4
|
1.0
|
C5'
|
C:IMP920
|
2.7
|
20.9
|
1.0
|
NH2
|
C:ARG309
|
3.4
|
43.8
|
1.0
|
NH2
|
C:ARG310
|
3.6
|
7.4
|
1.0
|
NE
|
C:ARG310
|
3.6
|
9.4
|
1.0
|
OH
|
C:TYR75
|
3.6
|
53.1
|
1.0
|
C4'
|
C:IMP920
|
4.1
|
17.0
|
1.0
|
CZ
|
C:ARG310
|
4.1
|
8.1
|
1.0
|
O4'
|
C:IMP920
|
4.3
|
19.4
|
1.0
|
CE1
|
C:TYR75
|
4.3
|
46.3
|
1.0
|
CZ
|
C:TYR75
|
4.4
|
49.2
|
1.0
|
CD
|
C:ARG310
|
4.7
|
8.1
|
1.0
|
CZ
|
C:ARG309
|
4.7
|
39.1
|
1.0
|
C8
|
C:IMP920
|
4.7
|
21.9
|
1.0
|
C3'
|
C:IMP920
|
4.8
|
20.6
|
1.0
|
|
Phosphorus binding site 10 out
of 12 in 1abb
Go back to
Phosphorus Binding Sites List in 1abb
Phosphorus binding site 10 out
of 12 in the Control of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies on R-State Glycogen Phosphorylase Reconstituted with Pyridoxal 5'-Diphosphate
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 10 of Control of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies on R-State Glycogen Phosphorylase Reconstituted with Pyridoxal 5'-Diphosphate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:P934
b:26.1
occ:1.00
|
PA
|
D:PDP934
|
0.0
|
26.1
|
1.0
|
O1A
|
D:PDP934
|
1.5
|
26.3
|
1.0
|
O2A
|
D:PDP934
|
1.5
|
22.1
|
1.0
|
O5A
|
D:PDP934
|
1.6
|
31.0
|
1.0
|
O3A
|
D:PDP934
|
1.7
|
45.2
|
1.0
|
C5A
|
D:PDP934
|
2.7
|
31.3
|
1.0
|
PB
|
D:PDP934
|
3.0
|
58.7
|
1.0
|
O3B
|
D:PDP934
|
3.3
|
60.5
|
1.0
|
NZ
|
D:LYS568
|
3.4
|
22.3
|
1.0
|
N
|
D:GLY677
|
3.4
|
2.0
|
1.0
|
O2B
|
D:PDP934
|
3.5
|
58.2
|
1.0
|
CA
|
D:GLY677
|
3.8
|
9.2
|
1.0
|
C5
|
D:PDP934
|
4.0
|
26.0
|
1.0
|
O1B
|
D:PDP934
|
4.1
|
59.1
|
1.0
|
CE
|
D:LYS568
|
4.3
|
24.5
|
1.0
|
N
|
D:THR676
|
4.4
|
21.9
|
1.0
|
C
|
D:THR676
|
4.6
|
7.7
|
1.0
|
C6
|
D:PDP934
|
4.6
|
22.0
|
1.0
|
CD
|
D:LYS568
|
4.6
|
19.7
|
1.0
|
CA
|
D:GLY675
|
4.9
|
29.4
|
1.0
|
C4
|
D:PDP934
|
4.9
|
23.8
|
1.0
|
CB
|
D:THR676
|
4.9
|
15.7
|
1.0
|
OD1
|
D:ASN678
|
4.9
|
32.4
|
1.0
|
CA
|
D:THR676
|
5.0
|
10.4
|
1.0
|
C
|
D:GLY677
|
5.0
|
9.7
|
1.0
|
|
Reference:
D.D.Leonidas,
N.G.Oikonomakos,
A.C.Papageorgiou,
K.R.Acharya,
D.Barford,
L.N.Johnson.
Control of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies on R-State Glycogen Phosphorylase Reconstituted with Pyridoxal 5'-Diphosphate. Protein Sci. V. 1 1112 1992.
ISSN: ISSN 0961-8368
PubMed: 1304390
Page generated: Fri Sep 25 12:42:20 2020
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