Magnesium in PDB 1zyk: Anthranilate Phosphoribosyltransferase in Complex with Prpp, Anthranilate and Magnesium
Enzymatic activity of Anthranilate Phosphoribosyltransferase in Complex with Prpp, Anthranilate and Magnesium
All present enzymatic activity of Anthranilate Phosphoribosyltransferase in Complex with Prpp, Anthranilate and Magnesium:
2.4.2.18;
Protein crystallography data
The structure of Anthranilate Phosphoribosyltransferase in Complex with Prpp, Anthranilate and Magnesium, PDB code: 1zyk
was solved by
M.Marino,
M.Deuss,
R.Sterner,
O.Mayans,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
20.00 /
2.40
|
Space group
|
P 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
92.556,
66.099,
117.069,
90.00,
107.76,
90.00
|
R / Rfree (%)
|
20.7 /
26.9
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Anthranilate Phosphoribosyltransferase in Complex with Prpp, Anthranilate and Magnesium
(pdb code 1zyk). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 8 binding sites of Magnesium where determined in the
Anthranilate Phosphoribosyltransferase in Complex with Prpp, Anthranilate and Magnesium, PDB code: 1zyk:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Magnesium binding site 1 out
of 8 in 1zyk
Go back to
Magnesium Binding Sites List in 1zyk
Magnesium binding site 1 out
of 8 in the Anthranilate Phosphoribosyltransferase in Complex with Prpp, Anthranilate and Magnesium
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Anthranilate Phosphoribosyltransferase in Complex with Prpp, Anthranilate and Magnesium within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg701
b:70.0
occ:1.00
|
O2B
|
A:PRP601
|
1.5
|
29.7
|
1.0
|
O4
|
A:PRP601
|
1.9
|
58.7
|
1.0
|
O2
|
A:PRP601
|
1.9
|
56.1
|
1.0
|
PB
|
A:PRP601
|
2.1
|
30.5
|
1.0
|
C4
|
A:PRP601
|
2.2
|
61.0
|
1.0
|
C1
|
A:PRP601
|
2.3
|
52.8
|
1.0
|
C2
|
A:PRP601
|
2.3
|
54.9
|
1.0
|
O3A
|
A:PRP601
|
2.4
|
39.1
|
1.0
|
O1
|
A:PRP601
|
2.5
|
46.0
|
1.0
|
O1B
|
A:PRP601
|
2.6
|
34.9
|
1.0
|
C3
|
A:PRP601
|
2.7
|
59.4
|
1.0
|
PA
|
A:PRP601
|
3.1
|
36.6
|
1.0
|
O3
|
A:PRP601
|
3.2
|
57.8
|
1.0
|
N
|
A:GLY79
|
3.4
|
24.2
|
1.0
|
O3B
|
A:PRP601
|
3.5
|
39.2
|
1.0
|
C5
|
A:PRP601
|
3.6
|
66.9
|
1.0
|
O
|
A:HOH957
|
3.8
|
56.2
|
1.0
|
CB
|
A:SER91
|
3.9
|
25.3
|
1.0
|
OG
|
A:SER91
|
4.0
|
30.2
|
1.0
|
CA
|
A:GLY79
|
4.0
|
26.4
|
1.0
|
O2A
|
A:PRP601
|
4.0
|
42.3
|
1.0
|
O1A
|
A:PRP601
|
4.1
|
40.3
|
1.0
|
MG
|
A:MG702
|
4.2
|
81.6
|
1.0
|
O
|
A:GLY79
|
4.3
|
28.0
|
1.0
|
C
|
A:ALA78
|
4.3
|
25.3
|
1.0
|
CA
|
A:ALA78
|
4.4
|
26.6
|
1.0
|
C
|
A:GLY79
|
4.5
|
28.8
|
1.0
|
O
|
A:THR77
|
4.6
|
27.0
|
1.0
|
O5
|
A:PRP601
|
4.6
|
73.3
|
1.0
|
OD2
|
A:ASP223
|
4.6
|
28.7
|
1.0
|
O
|
A:HOH862
|
4.7
|
13.7
|
1.0
|
O
|
A:HOH813
|
4.8
|
25.3
|
1.0
|
OE1
|
A:GLU224
|
4.9
|
46.9
|
1.0
|
O3P
|
A:PRP601
|
4.9
|
77.2
|
1.0
|
|
Magnesium binding site 2 out
of 8 in 1zyk
Go back to
Magnesium Binding Sites List in 1zyk
Magnesium binding site 2 out
of 8 in the Anthranilate Phosphoribosyltransferase in Complex with Prpp, Anthranilate and Magnesium
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Anthranilate Phosphoribosyltransferase in Complex with Prpp, Anthranilate and Magnesium within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg702
b:81.6
occ:1.00
|
OE1
|
A:GLU224
|
1.7
|
46.9
|
1.0
|
O5
|
A:PRP601
|
1.9
|
73.3
|
1.0
|
O3P
|
A:PRP601
|
2.2
|
77.2
|
1.0
|
C3
|
A:PRP601
|
2.4
|
59.4
|
1.0
|
CD
|
A:GLU224
|
2.4
|
44.0
|
1.0
|
P
|
A:PRP601
|
2.4
|
79.9
|
1.0
|
C1
|
A:PRP601
|
2.6
|
52.8
|
1.0
|
C4
|
A:PRP601
|
2.7
|
61.0
|
1.0
|
C5
|
A:PRP601
|
2.7
|
66.9
|
1.0
|
O4
|
A:PRP601
|
2.8
|
58.7
|
1.0
|
C2
|
A:PRP601
|
2.8
|
54.9
|
1.0
|
O2P
|
A:PRP601
|
3.0
|
79.3
|
1.0
|
CG
|
A:GLU224
|
3.0
|
38.2
|
1.0
|
OE2
|
A:GLU224
|
3.3
|
44.0
|
1.0
|
OD1
|
A:ASP223
|
3.4
|
29.2
|
1.0
|
O3
|
A:PRP601
|
3.7
|
57.8
|
1.0
|
O1P
|
A:PRP601
|
3.8
|
78.7
|
1.0
|
O1
|
A:PRP601
|
3.9
|
46.0
|
1.0
|
O
|
A:ASP223
|
4.0
|
27.4
|
1.0
|
CG1
|
A:VAL90
|
4.2
|
19.4
|
1.0
|
O2
|
A:PRP601
|
4.2
|
56.1
|
1.0
|
CG
|
A:ASP223
|
4.2
|
30.2
|
1.0
|
OG1
|
A:THR87
|
4.2
|
29.3
|
1.0
|
MG
|
A:MG701
|
4.2
|
70.0
|
1.0
|
CB
|
A:GLU224
|
4.4
|
34.1
|
1.0
|
OD2
|
A:ASP223
|
4.5
|
28.7
|
1.0
|
OD2
|
A:ASP83
|
4.5
|
57.5
|
1.0
|
C
|
A:ASP223
|
4.6
|
29.1
|
1.0
|
O1A
|
A:PRP601
|
4.8
|
40.3
|
1.0
|
O
|
A:HOH957
|
4.9
|
56.2
|
1.0
|
PA
|
A:PRP601
|
4.9
|
36.6
|
1.0
|
|
Magnesium binding site 3 out
of 8 in 1zyk
Go back to
Magnesium Binding Sites List in 1zyk
Magnesium binding site 3 out
of 8 in the Anthranilate Phosphoribosyltransferase in Complex with Prpp, Anthranilate and Magnesium
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Anthranilate Phosphoribosyltransferase in Complex with Prpp, Anthranilate and Magnesium within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg703
b:71.7
occ:1.00
|
O2B
|
B:PRP602
|
1.5
|
44.7
|
1.0
|
O4
|
B:PRP602
|
1.9
|
69.7
|
1.0
|
O2
|
B:PRP602
|
2.0
|
69.6
|
1.0
|
PB
|
B:PRP602
|
2.1
|
46.5
|
1.0
|
C4
|
B:PRP602
|
2.2
|
71.3
|
1.0
|
C1
|
B:PRP602
|
2.3
|
65.2
|
1.0
|
C2
|
B:PRP602
|
2.3
|
66.8
|
1.0
|
O3A
|
B:PRP602
|
2.4
|
52.2
|
1.0
|
O1
|
B:PRP602
|
2.5
|
60.3
|
1.0
|
O1B
|
B:PRP602
|
2.5
|
50.5
|
1.0
|
C3
|
B:PRP602
|
2.7
|
69.6
|
1.0
|
PA
|
B:PRP602
|
3.1
|
51.3
|
1.0
|
O3
|
B:PRP602
|
3.2
|
68.6
|
1.0
|
N
|
B:GLY79
|
3.3
|
26.3
|
1.0
|
O3B
|
B:PRP602
|
3.5
|
51.6
|
1.0
|
C5
|
B:PRP602
|
3.6
|
74.8
|
1.0
|
CB
|
B:SER91
|
3.9
|
28.5
|
1.0
|
O2A
|
B:PRP602
|
4.0
|
57.4
|
1.0
|
CA
|
B:GLY79
|
4.0
|
30.0
|
1.0
|
OG
|
B:SER91
|
4.0
|
33.2
|
1.0
|
O1A
|
B:PRP602
|
4.1
|
53.4
|
1.0
|
CA
|
B:ALA78
|
4.2
|
27.6
|
1.0
|
C
|
B:ALA78
|
4.2
|
27.1
|
1.0
|
O
|
B:GLY79
|
4.3
|
31.6
|
1.0
|
MG
|
B:MG704
|
4.3
|
53.7
|
1.0
|
O
|
B:THR77
|
4.5
|
27.8
|
1.0
|
C
|
B:GLY79
|
4.5
|
31.1
|
1.0
|
O5
|
B:PRP602
|
4.6
|
78.0
|
1.0
|
NZ
|
B:LYS106
|
4.7
|
28.7
|
1.0
|
OD2
|
B:ASP223
|
4.7
|
29.6
|
1.0
|
OE2
|
B:GLU224
|
4.8
|
38.2
|
1.0
|
O
|
B:HOH816
|
4.8
|
24.1
|
1.0
|
O3P
|
B:PRP602
|
4.9
|
80.2
|
1.0
|
O
|
B:HOH887
|
4.9
|
38.4
|
1.0
|
O
|
B:HOH829
|
4.9
|
21.0
|
1.0
|
O
|
B:HOH867
|
5.0
|
31.0
|
1.0
|
|
Magnesium binding site 4 out
of 8 in 1zyk
Go back to
Magnesium Binding Sites List in 1zyk
Magnesium binding site 4 out
of 8 in the Anthranilate Phosphoribosyltransferase in Complex with Prpp, Anthranilate and Magnesium
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Anthranilate Phosphoribosyltransferase in Complex with Prpp, Anthranilate and Magnesium within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg704
b:53.7
occ:1.00
|
OE2
|
B:GLU224
|
1.9
|
38.2
|
1.0
|
O5
|
B:PRP602
|
1.9
|
78.0
|
1.0
|
O3P
|
B:PRP602
|
2.2
|
80.2
|
1.0
|
CD
|
B:GLU224
|
2.3
|
35.2
|
1.0
|
C3
|
B:PRP602
|
2.4
|
69.6
|
1.0
|
P
|
B:PRP602
|
2.4
|
82.5
|
1.0
|
C1
|
B:PRP602
|
2.6
|
65.2
|
1.0
|
CG
|
B:GLU224
|
2.6
|
31.0
|
1.0
|
C4
|
B:PRP602
|
2.7
|
71.3
|
1.0
|
C5
|
B:PRP602
|
2.7
|
74.8
|
1.0
|
O4
|
B:PRP602
|
2.8
|
69.7
|
1.0
|
C2
|
B:PRP602
|
2.8
|
66.8
|
1.0
|
O2P
|
B:PRP602
|
3.0
|
80.5
|
1.0
|
OE1
|
B:GLU224
|
3.2
|
37.7
|
1.0
|
OD1
|
B:ASP223
|
3.5
|
28.2
|
1.0
|
O
|
B:ASP223
|
3.7
|
23.9
|
1.0
|
O3
|
B:PRP602
|
3.7
|
68.6
|
1.0
|
O1P
|
B:PRP602
|
3.8
|
81.9
|
1.0
|
O1
|
B:PRP602
|
3.9
|
60.3
|
1.0
|
CB
|
B:GLU224
|
4.1
|
26.3
|
1.0
|
CG1
|
B:VAL90
|
4.1
|
19.9
|
1.0
|
O2
|
B:PRP602
|
4.2
|
69.6
|
1.0
|
CG
|
B:ASP223
|
4.2
|
29.3
|
1.0
|
MG
|
B:MG703
|
4.3
|
71.7
|
1.0
|
C
|
B:ASP223
|
4.3
|
26.0
|
1.0
|
OD2
|
B:ASP223
|
4.5
|
29.6
|
1.0
|
OG1
|
B:THR87
|
4.6
|
36.4
|
1.0
|
O1A
|
B:PRP602
|
4.7
|
53.4
|
1.0
|
CA
|
B:GLU224
|
4.8
|
24.9
|
1.0
|
N
|
B:GLU224
|
4.8
|
25.5
|
1.0
|
OD2
|
B:ASP83
|
4.9
|
52.0
|
1.0
|
O
|
B:HOH902
|
4.9
|
41.6
|
1.0
|
PA
|
B:PRP602
|
4.9
|
51.3
|
1.0
|
|
Magnesium binding site 5 out
of 8 in 1zyk
Go back to
Magnesium Binding Sites List in 1zyk
Magnesium binding site 5 out
of 8 in the Anthranilate Phosphoribosyltransferase in Complex with Prpp, Anthranilate and Magnesium
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of Anthranilate Phosphoribosyltransferase in Complex with Prpp, Anthranilate and Magnesium within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg705
b:70.9
occ:1.00
|
O2B
|
C:PRP603
|
1.5
|
62.6
|
1.0
|
O4
|
C:PRP603
|
1.9
|
74.8
|
1.0
|
O2
|
C:PRP603
|
1.9
|
72.7
|
1.0
|
PB
|
C:PRP603
|
2.1
|
62.6
|
1.0
|
C4
|
C:PRP603
|
2.2
|
75.9
|
1.0
|
C1
|
C:PRP603
|
2.3
|
71.5
|
1.0
|
C2
|
C:PRP603
|
2.3
|
72.5
|
1.0
|
O3A
|
C:PRP603
|
2.4
|
65.6
|
1.0
|
O1
|
C:PRP603
|
2.5
|
69.7
|
1.0
|
O1B
|
C:PRP603
|
2.6
|
64.4
|
1.0
|
C3
|
C:PRP603
|
2.7
|
74.4
|
1.0
|
PA
|
C:PRP603
|
3.1
|
63.6
|
1.0
|
O3
|
C:PRP603
|
3.2
|
73.2
|
1.0
|
N
|
C:GLY79
|
3.2
|
29.6
|
1.0
|
O3B
|
C:PRP603
|
3.5
|
67.3
|
1.0
|
C5
|
C:PRP603
|
3.6
|
79.3
|
1.0
|
CB
|
C:SER91
|
3.9
|
27.1
|
1.0
|
CA
|
C:GLY79
|
3.9
|
30.6
|
1.0
|
O
|
C:GLY79
|
4.0
|
33.4
|
1.0
|
O2A
|
C:PRP603
|
4.0
|
66.4
|
1.0
|
OG
|
C:SER91
|
4.0
|
37.2
|
1.0
|
C
|
C:ALA78
|
4.1
|
29.3
|
1.0
|
O1A
|
C:PRP603
|
4.1
|
66.4
|
1.0
|
CA
|
C:ALA78
|
4.1
|
29.7
|
1.0
|
MG
|
C:MG706
|
4.3
|
78.8
|
1.0
|
C
|
C:GLY79
|
4.4
|
32.4
|
1.0
|
O
|
C:THR77
|
4.4
|
27.1
|
1.0
|
O5
|
C:PRP603
|
4.6
|
84.4
|
1.0
|
O3P
|
C:PRP603
|
4.9
|
87.1
|
1.0
|
OD2
|
C:ASP223
|
4.9
|
34.5
|
1.0
|
OE1
|
C:GLU224
|
4.9
|
45.9
|
1.0
|
O
|
C:HOH828
|
5.0
|
26.2
|
1.0
|
CB
|
C:ALA78
|
5.0
|
31.4
|
1.0
|
NZ
|
C:LYS106
|
5.0
|
21.7
|
1.0
|
|
Magnesium binding site 6 out
of 8 in 1zyk
Go back to
Magnesium Binding Sites List in 1zyk
Magnesium binding site 6 out
of 8 in the Anthranilate Phosphoribosyltransferase in Complex with Prpp, Anthranilate and Magnesium
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 6 of Anthranilate Phosphoribosyltransferase in Complex with Prpp, Anthranilate and Magnesium within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg706
b:78.8
occ:1.00
|
OE1
|
C:GLU224
|
1.8
|
45.9
|
1.0
|
O5
|
C:PRP603
|
1.9
|
84.4
|
1.0
|
O3P
|
C:PRP603
|
2.2
|
87.1
|
1.0
|
CD
|
C:GLU224
|
2.2
|
39.9
|
1.0
|
C3
|
C:PRP603
|
2.4
|
74.4
|
1.0
|
P
|
C:PRP603
|
2.4
|
88.2
|
1.0
|
C1
|
C:PRP603
|
2.6
|
71.5
|
1.0
|
CG
|
C:GLU224
|
2.7
|
35.3
|
1.0
|
C4
|
C:PRP603
|
2.7
|
75.9
|
1.0
|
C5
|
C:PRP603
|
2.7
|
79.3
|
1.0
|
O4
|
C:PRP603
|
2.8
|
74.8
|
1.0
|
C2
|
C:PRP603
|
2.8
|
72.5
|
1.0
|
O2P
|
C:PRP603
|
3.0
|
86.8
|
1.0
|
OE2
|
C:GLU224
|
3.1
|
40.9
|
1.0
|
OD1
|
C:ASP223
|
3.4
|
32.4
|
1.0
|
O
|
C:ASP223
|
3.7
|
26.5
|
1.0
|
O3
|
C:PRP603
|
3.7
|
73.2
|
1.0
|
O1P
|
C:PRP603
|
3.8
|
88.1
|
1.0
|
O1
|
C:PRP603
|
4.0
|
69.7
|
1.0
|
CG
|
C:ASP223
|
4.0
|
32.3
|
1.0
|
CB
|
C:GLU224
|
4.1
|
31.2
|
1.0
|
O2
|
C:PRP603
|
4.2
|
72.7
|
1.0
|
C
|
C:ASP223
|
4.2
|
28.8
|
1.0
|
MG
|
C:MG705
|
4.3
|
70.9
|
1.0
|
OD2
|
C:ASP223
|
4.3
|
34.5
|
1.0
|
CG1
|
C:VAL90
|
4.4
|
24.6
|
1.0
|
OD2
|
C:ASP83
|
4.7
|
49.3
|
1.0
|
N
|
C:GLU224
|
4.7
|
29.6
|
1.0
|
OG1
|
C:THR87
|
4.7
|
34.9
|
1.0
|
CA
|
C:GLU224
|
4.7
|
29.2
|
1.0
|
CG1
|
C:ILE222
|
4.7
|
28.3
|
1.0
|
O1A
|
C:PRP603
|
4.8
|
66.4
|
1.0
|
PA
|
C:PRP603
|
5.0
|
63.6
|
1.0
|
O
|
C:HOH825
|
5.0
|
19.7
|
1.0
|
|
Magnesium binding site 7 out
of 8 in 1zyk
Go back to
Magnesium Binding Sites List in 1zyk
Magnesium binding site 7 out
of 8 in the Anthranilate Phosphoribosyltransferase in Complex with Prpp, Anthranilate and Magnesium
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 7 of Anthranilate Phosphoribosyltransferase in Complex with Prpp, Anthranilate and Magnesium within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg707
b:43.8
occ:1.00
|
O2B
|
D:PRP604
|
1.5
|
41.7
|
1.0
|
O2
|
D:PRP604
|
1.9
|
55.6
|
1.0
|
O4
|
D:PRP604
|
1.9
|
59.8
|
1.0
|
PB
|
D:PRP604
|
2.1
|
41.6
|
1.0
|
C4
|
D:PRP604
|
2.3
|
61.1
|
1.0
|
C1
|
D:PRP604
|
2.3
|
55.6
|
1.0
|
C2
|
D:PRP604
|
2.3
|
55.8
|
1.0
|
O3A
|
D:PRP604
|
2.4
|
47.4
|
1.0
|
O1
|
D:PRP604
|
2.5
|
51.9
|
1.0
|
O1B
|
D:PRP604
|
2.6
|
48.1
|
1.0
|
C3
|
D:PRP604
|
2.7
|
59.3
|
1.0
|
PA
|
D:PRP604
|
3.1
|
44.5
|
1.0
|
N
|
D:GLY79
|
3.1
|
27.9
|
1.0
|
O3
|
D:PRP604
|
3.2
|
58.3
|
1.0
|
O3B
|
D:PRP604
|
3.5
|
50.3
|
1.0
|
C5
|
D:PRP604
|
3.6
|
64.0
|
1.0
|
CA
|
D:GLY79
|
3.8
|
29.5
|
1.0
|
CB
|
D:SER91
|
3.8
|
29.4
|
1.0
|
O2A
|
D:PRP604
|
4.0
|
50.1
|
1.0
|
C
|
D:ALA78
|
4.0
|
26.2
|
1.0
|
OG
|
D:SER91
|
4.1
|
34.8
|
1.0
|
CA
|
D:ALA78
|
4.1
|
28.3
|
1.0
|
O1A
|
D:PRP604
|
4.1
|
47.1
|
1.0
|
MG
|
D:MG708
|
4.3
|
89.3
|
1.0
|
O
|
D:THR77
|
4.4
|
31.7
|
1.0
|
O
|
D:GLY79
|
4.4
|
33.4
|
1.0
|
C
|
D:GLY79
|
4.5
|
31.8
|
1.0
|
O
|
D:HOH862
|
4.5
|
31.6
|
1.0
|
O5
|
D:PRP604
|
4.6
|
67.3
|
1.0
|
O3P
|
D:PRP604
|
4.9
|
70.5
|
1.0
|
NZ
|
D:LYS106
|
4.9
|
24.1
|
1.0
|
CB
|
D:ALA78
|
4.9
|
25.8
|
1.0
|
OE1
|
D:GLU224
|
4.9
|
40.4
|
1.0
|
O
|
D:HOH933
|
5.0
|
56.7
|
1.0
|
OD2
|
D:ASP223
|
5.0
|
47.8
|
1.0
|
|
Magnesium binding site 8 out
of 8 in 1zyk
Go back to
Magnesium Binding Sites List in 1zyk
Magnesium binding site 8 out
of 8 in the Anthranilate Phosphoribosyltransferase in Complex with Prpp, Anthranilate and Magnesium
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 8 of Anthranilate Phosphoribosyltransferase in Complex with Prpp, Anthranilate and Magnesium within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg708
b:89.3
occ:1.00
|
OE1
|
D:GLU224
|
1.7
|
40.4
|
1.0
|
O5
|
D:PRP604
|
1.9
|
67.3
|
1.0
|
O3P
|
D:PRP604
|
2.2
|
70.5
|
1.0
|
CD
|
D:GLU224
|
2.3
|
40.0
|
1.0
|
C3
|
D:PRP604
|
2.4
|
59.3
|
1.0
|
P
|
D:PRP604
|
2.4
|
72.2
|
1.0
|
C1
|
D:PRP604
|
2.6
|
55.6
|
1.0
|
C4
|
D:PRP604
|
2.7
|
61.1
|
1.0
|
C5
|
D:PRP604
|
2.7
|
64.0
|
1.0
|
O4
|
D:PRP604
|
2.8
|
59.8
|
1.0
|
C2
|
D:PRP604
|
2.8
|
55.8
|
1.0
|
CG
|
D:GLU224
|
3.0
|
40.1
|
1.0
|
O2P
|
D:PRP604
|
3.0
|
71.1
|
1.0
|
OE2
|
D:GLU224
|
3.1
|
37.7
|
1.0
|
OD1
|
D:ASP223
|
3.6
|
52.2
|
1.0
|
O
|
D:ASP223
|
3.7
|
40.9
|
1.0
|
O3
|
D:PRP604
|
3.7
|
58.3
|
1.0
|
O1P
|
D:PRP604
|
3.8
|
71.6
|
1.0
|
O1
|
D:PRP604
|
4.0
|
51.9
|
1.0
|
CG
|
D:ASP223
|
4.1
|
48.1
|
1.0
|
O2
|
D:PRP604
|
4.2
|
55.6
|
1.0
|
C
|
D:ASP223
|
4.2
|
42.4
|
1.0
|
OD2
|
D:ASP223
|
4.3
|
47.8
|
1.0
|
MG
|
D:MG707
|
4.3
|
43.8
|
1.0
|
CG1
|
D:VAL90
|
4.3
|
24.2
|
1.0
|
CB
|
D:GLU224
|
4.4
|
40.4
|
1.0
|
OG1
|
D:THR87
|
4.5
|
35.4
|
1.0
|
OD2
|
D:ASP83
|
4.6
|
51.6
|
1.0
|
N
|
D:GLU224
|
4.8
|
42.0
|
1.0
|
O1A
|
D:PRP604
|
4.8
|
47.1
|
1.0
|
N
|
D:ASP223
|
4.8
|
41.9
|
1.0
|
CA
|
D:GLU224
|
4.9
|
41.1
|
1.0
|
CA
|
D:ASP223
|
4.9
|
43.5
|
1.0
|
PA
|
D:PRP604
|
5.0
|
44.5
|
1.0
|
|
Reference:
M.Marino,
M.Deuss,
D.I.Svergun,
P.V.Konarev,
R.Sterner,
O.Mayans.
Structural and Mutational Analysis of Substrate Complexation By Anthranilate Phosphoribosyltransferase From Sulfolobus Solfataricus. J.Biol.Chem. V. 281 21410 2006.
ISSN: ISSN 0021-9258
PubMed: 16714288
DOI: 10.1074/JBC.M601403200
Page generated: Tue Aug 13 20:16:16 2024
|