Phosphorus in PDB 1a96: Xprtase From E. Coli with Bound Cprpp and Xanthine
Enzymatic activity of Xprtase From E. Coli with Bound Cprpp and Xanthine
All present enzymatic activity of Xprtase From E. Coli with Bound Cprpp and Xanthine:
2.4.2.22;
Protein crystallography data
The structure of Xprtase From E. Coli with Bound Cprpp and Xanthine, PDB code: 1a96
was solved by
S.Vos,
R.J.Parry,
M.R.Burns,
J.De Jersey,
J.L.Martin,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
50.00 /
2.00
|
Space group
|
P 43 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
94.200,
94.200,
165.900,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
21.8 /
24.4
|
Phosphorus Binding Sites:
The binding sites of Phosphorus atom in the Xprtase From E. Coli with Bound Cprpp and Xanthine
(pdb code 1a96). This binding sites where shown within
5.0 Angstroms radius around Phosphorus atom.
In total 6 binding sites of Phosphorus where determined in the
Xprtase From E. Coli with Bound Cprpp and Xanthine, PDB code: 1a96:
Jump to Phosphorus binding site number:
1;
2;
3;
4;
5;
6;
Phosphorus binding site 1 out
of 6 in 1a96
Go back to
Phosphorus Binding Sites List in 1a96
Phosphorus binding site 1 out
of 6 in the Xprtase From E. Coli with Bound Cprpp and Xanthine
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 1 of Xprtase From E. Coli with Bound Cprpp and Xanthine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:P301
b:54.0
occ:1.00
|
P
|
B:PCP301
|
0.0
|
54.0
|
1.0
|
O2P
|
B:PCP301
|
1.5
|
54.6
|
1.0
|
O1P
|
B:PCP301
|
1.5
|
52.1
|
1.0
|
O3P
|
B:PCP301
|
1.5
|
54.4
|
1.0
|
OP
|
B:PCP301
|
1.6
|
62.9
|
1.0
|
CP
|
B:PCP301
|
2.7
|
74.2
|
1.0
|
OG1
|
B:THR93
|
3.5
|
28.0
|
1.0
|
NH2
|
B:ARG69
|
3.5
|
50.7
|
1.0
|
O
|
B:HOH443
|
3.7
|
23.4
|
1.0
|
N
|
B:THR93
|
3.8
|
26.6
|
1.0
|
C4
|
B:PCP301
|
3.8
|
82.7
|
1.0
|
CB
|
B:ASP92
|
3.8
|
29.8
|
1.0
|
N
|
B:ASP92
|
4.0
|
24.4
|
1.0
|
N
|
B:GLY94
|
4.1
|
25.6
|
1.0
|
OG1
|
B:THR96
|
4.1
|
28.0
|
1.0
|
N
|
B:GLY95
|
4.1
|
25.3
|
1.0
|
N
|
B:THR96
|
4.3
|
24.2
|
1.0
|
CA
|
B:ASP92
|
4.4
|
26.3
|
1.0
|
C5
|
B:PCP301
|
4.4
|
87.1
|
1.0
|
CB
|
B:THR93
|
4.6
|
29.5
|
1.0
|
C
|
B:ASP92
|
4.6
|
26.6
|
1.0
|
CA
|
B:THR93
|
4.6
|
27.7
|
1.0
|
CB
|
B:THR96
|
4.8
|
25.9
|
1.0
|
CA
|
B:GLY95
|
4.8
|
25.1
|
1.0
|
CZ
|
B:ARG69
|
4.8
|
51.0
|
1.0
|
CA
|
B:GLY94
|
4.8
|
24.7
|
1.0
|
C
|
B:THR93
|
4.8
|
27.7
|
1.0
|
C
|
B:GLY94
|
4.9
|
24.9
|
1.0
|
C8
|
B:XAN304
|
4.9
|
38.7
|
1.0
|
CG
|
B:ASP92
|
5.0
|
34.2
|
1.0
|
|
Phosphorus binding site 2 out
of 6 in 1a96
Go back to
Phosphorus Binding Sites List in 1a96
Phosphorus binding site 2 out
of 6 in the Xprtase From E. Coli with Bound Cprpp and Xanthine
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 2 of Xprtase From E. Coli with Bound Cprpp and Xanthine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:P301
b:0.0
occ:1.00
|
PA
|
B:PCP301
|
0.0
|
0.0
|
1.0
|
O2A
|
B:PCP301
|
1.5
|
0.0
|
1.0
|
O1A
|
B:PCP301
|
1.5
|
0.0
|
1.0
|
O3A
|
B:PCP301
|
1.5
|
0.0
|
1.0
|
O1
|
B:PCP301
|
1.6
|
97.0
|
1.0
|
C1
|
B:PCP301
|
2.7
|
90.6
|
1.0
|
PB
|
B:PCP301
|
2.8
|
0.0
|
1.0
|
C5
|
B:PCP301
|
3.1
|
87.1
|
1.0
|
O2B
|
B:PCP301
|
3.2
|
0.0
|
1.0
|
MG
|
B:MG308
|
3.3
|
57.1
|
1.0
|
O
|
B:HOH541
|
3.6
|
56.9
|
1.0
|
O1B
|
B:PCP301
|
3.7
|
99.2
|
1.0
|
NH2
|
A:ARG53
|
3.9
|
34.6
|
0.5
|
O3B
|
B:PCP301
|
3.9
|
0.0
|
1.0
|
C2
|
B:PCP301
|
4.0
|
88.4
|
1.0
|
O2
|
B:PCP301
|
4.2
|
88.5
|
1.0
|
C4
|
B:PCP301
|
4.4
|
82.7
|
1.0
|
C3
|
B:PCP301
|
4.6
|
85.9
|
1.0
|
O3
|
B:PCP301
|
4.6
|
85.4
|
1.0
|
|
Phosphorus binding site 3 out
of 6 in 1a96
Go back to
Phosphorus Binding Sites List in 1a96
Phosphorus binding site 3 out
of 6 in the Xprtase From E. Coli with Bound Cprpp and Xanthine
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 3 of Xprtase From E. Coli with Bound Cprpp and Xanthine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:P301
b:0.0
occ:1.00
|
PB
|
B:PCP301
|
0.0
|
0.0
|
1.0
|
O2B
|
B:PCP301
|
1.4
|
0.0
|
1.0
|
O1B
|
B:PCP301
|
1.5
|
99.2
|
1.0
|
O3B
|
B:PCP301
|
1.5
|
0.0
|
1.0
|
O3A
|
B:PCP301
|
1.5
|
0.0
|
1.0
|
PA
|
B:PCP301
|
2.8
|
0.0
|
1.0
|
O1
|
B:PCP301
|
3.1
|
97.0
|
1.0
|
NH2
|
A:ARG53
|
3.3
|
34.6
|
0.5
|
MG
|
B:MG308
|
3.3
|
57.1
|
1.0
|
O2A
|
B:PCP301
|
3.6
|
0.0
|
1.0
|
O
|
B:HOH541
|
3.6
|
56.9
|
1.0
|
N
|
B:ARG37
|
3.6
|
17.6
|
1.0
|
NE
|
B:ARG37
|
3.9
|
26.0
|
1.0
|
O1A
|
B:PCP301
|
4.0
|
0.0
|
1.0
|
N
|
B:GLY38
|
4.2
|
14.3
|
1.0
|
NH2
|
B:ARG37
|
4.2
|
28.4
|
1.0
|
CB
|
B:ARG37
|
4.2
|
18.1
|
1.0
|
CZ
|
A:ARG53
|
4.2
|
35.1
|
0.5
|
CA
|
B:ARG37
|
4.4
|
17.4
|
1.0
|
NH1
|
A:ARG53
|
4.4
|
35.0
|
0.5
|
C1
|
B:PCP301
|
4.5
|
90.6
|
1.0
|
CZ
|
B:ARG37
|
4.5
|
26.2
|
1.0
|
O
|
B:SER36
|
4.5
|
19.9
|
1.0
|
C
|
B:SER36
|
4.5
|
19.1
|
1.0
|
O2
|
B:PCP301
|
4.5
|
88.5
|
1.0
|
O
|
B:HOH542
|
4.6
|
53.8
|
1.0
|
CG
|
B:ARG37
|
4.6
|
18.9
|
1.0
|
O
|
B:HOH459
|
4.7
|
36.4
|
1.0
|
C
|
B:ARG37
|
4.7
|
17.0
|
1.0
|
CD
|
B:ARG37
|
4.9
|
22.1
|
1.0
|
|
Phosphorus binding site 4 out
of 6 in 1a96
Go back to
Phosphorus Binding Sites List in 1a96
Phosphorus binding site 4 out
of 6 in the Xprtase From E. Coli with Bound Cprpp and Xanthine
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 4 of Xprtase From E. Coli with Bound Cprpp and Xanthine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:P302
b:40.5
occ:1.00
|
P
|
C:PCP302
|
0.0
|
40.5
|
1.0
|
O2P
|
C:PCP302
|
1.5
|
39.1
|
1.0
|
O1P
|
C:PCP302
|
1.5
|
37.0
|
1.0
|
O3P
|
C:PCP302
|
1.5
|
41.6
|
1.0
|
OP
|
C:PCP302
|
1.6
|
49.1
|
1.0
|
CP
|
C:PCP302
|
2.7
|
60.7
|
1.0
|
O
|
C:HOH485
|
3.4
|
34.1
|
1.0
|
NH2
|
C:ARG69
|
3.5
|
42.8
|
1.0
|
OG1
|
C:THR93
|
3.6
|
27.6
|
1.0
|
N
|
C:THR93
|
3.8
|
26.3
|
1.0
|
C4
|
C:PCP302
|
3.8
|
69.4
|
1.0
|
CB
|
C:ASP92
|
3.9
|
28.6
|
1.0
|
OG1
|
C:THR96
|
3.9
|
26.3
|
1.0
|
N
|
C:ASP92
|
4.0
|
25.4
|
1.0
|
N
|
C:GLY94
|
4.0
|
22.9
|
1.0
|
N
|
C:GLY95
|
4.1
|
24.0
|
1.0
|
NH1
|
C:ARG69
|
4.2
|
43.6
|
1.0
|
N
|
C:THR96
|
4.2
|
23.1
|
1.0
|
CZ
|
C:ARG69
|
4.3
|
42.1
|
1.0
|
CA
|
C:ASP92
|
4.3
|
26.3
|
1.0
|
C5
|
C:PCP302
|
4.5
|
73.9
|
1.0
|
C
|
C:ASP92
|
4.5
|
27.2
|
1.0
|
CB
|
C:THR96
|
4.6
|
23.9
|
1.0
|
CB
|
C:THR93
|
4.6
|
27.3
|
1.0
|
CA
|
C:THR93
|
4.6
|
26.1
|
1.0
|
CA
|
C:GLY95
|
4.7
|
23.4
|
1.0
|
CA
|
C:GLY94
|
4.8
|
22.5
|
1.0
|
C
|
C:GLY94
|
4.8
|
24.0
|
1.0
|
C
|
C:THR93
|
4.8
|
26.0
|
1.0
|
|
Phosphorus binding site 5 out
of 6 in 1a96
Go back to
Phosphorus Binding Sites List in 1a96
Phosphorus binding site 5 out
of 6 in the Xprtase From E. Coli with Bound Cprpp and Xanthine
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 5 of Xprtase From E. Coli with Bound Cprpp and Xanthine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:P302
b:88.1
occ:1.00
|
PA
|
C:PCP302
|
0.0
|
88.1
|
1.0
|
O2A
|
C:PCP302
|
1.5
|
87.2
|
1.0
|
O1A
|
C:PCP302
|
1.5
|
88.1
|
1.0
|
O3A
|
C:PCP302
|
1.5
|
86.4
|
1.0
|
O1
|
C:PCP302
|
1.6
|
83.7
|
1.0
|
C1
|
C:PCP302
|
2.7
|
77.3
|
1.0
|
PB
|
C:PCP302
|
2.8
|
82.9
|
1.0
|
C5
|
C:PCP302
|
3.1
|
73.9
|
1.0
|
O2B
|
C:PCP302
|
3.2
|
83.2
|
1.0
|
MG
|
C:MG307
|
3.3
|
57.9
|
1.0
|
O1B
|
C:PCP302
|
3.6
|
81.2
|
1.0
|
O3B
|
C:PCP302
|
3.9
|
84.1
|
1.0
|
C2
|
C:PCP302
|
4.0
|
75.1
|
1.0
|
O
|
C:HOH539
|
4.0
|
53.0
|
1.0
|
O2
|
C:PCP302
|
4.2
|
74.9
|
1.0
|
C4
|
C:PCP302
|
4.4
|
69.4
|
1.0
|
C3
|
C:PCP302
|
4.6
|
72.6
|
1.0
|
O3
|
C:PCP302
|
4.7
|
72.9
|
1.0
|
O
|
C:HOH467
|
5.0
|
46.6
|
1.0
|
|
Phosphorus binding site 6 out
of 6 in 1a96
Go back to
Phosphorus Binding Sites List in 1a96
Phosphorus binding site 6 out
of 6 in the Xprtase From E. Coli with Bound Cprpp and Xanthine
Mono view
Stereo pair view
|
A full contact list of Phosphorus with other atoms in the P binding
site number 6 of Xprtase From E. Coli with Bound Cprpp and Xanthine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:P302
b:82.9
occ:1.00
|
PB
|
C:PCP302
|
0.0
|
82.9
|
1.0
|
O2B
|
C:PCP302
|
1.4
|
83.2
|
1.0
|
O3B
|
C:PCP302
|
1.5
|
84.1
|
1.0
|
O1B
|
C:PCP302
|
1.5
|
81.2
|
1.0
|
O3A
|
C:PCP302
|
1.5
|
86.4
|
1.0
|
PA
|
C:PCP302
|
2.8
|
88.1
|
1.0
|
O1
|
C:PCP302
|
3.1
|
83.7
|
1.0
|
MG
|
C:MG307
|
3.5
|
57.9
|
1.0
|
O2A
|
C:PCP302
|
3.5
|
87.2
|
1.0
|
O
|
C:HOH539
|
3.9
|
53.0
|
1.0
|
NE
|
C:ARG37
|
4.0
|
27.9
|
1.0
|
O1A
|
C:PCP302
|
4.0
|
88.1
|
1.0
|
NH2
|
C:ARG37
|
4.0
|
29.6
|
1.0
|
N
|
C:ARG37
|
4.1
|
20.9
|
1.0
|
O
|
C:HOH451
|
4.2
|
24.7
|
1.0
|
N
|
C:GLY38
|
4.3
|
17.5
|
1.0
|
CB
|
C:ARG37
|
4.4
|
20.6
|
1.0
|
CZ
|
C:ARG37
|
4.5
|
29.9
|
1.0
|
C1
|
C:PCP302
|
4.5
|
77.3
|
1.0
|
O2
|
C:PCP302
|
4.6
|
74.9
|
1.0
|
CA
|
C:ARG37
|
4.7
|
19.0
|
1.0
|
O
|
C:HOH540
|
4.8
|
33.8
|
1.0
|
CG
|
C:ARG37
|
4.9
|
21.1
|
1.0
|
C
|
C:ARG37
|
4.9
|
19.4
|
1.0
|
O
|
C:HOH467
|
5.0
|
46.6
|
1.0
|
|
Reference:
S.Vos,
R.J.Parry,
M.R.Burns,
J.De Jersey,
J.L.Martin.
Structures of Free and Complexed Forms of Escherichia Coli Xanthine-Guanine Phosphoribosyltransferase. J.Mol.Biol. V. 282 875 1998.
ISSN: ISSN 0022-2836
PubMed: 9743633
DOI: 10.1006/JMBI.1998.2051
Page generated: Fri Sep 25 12:31:45 2020
|