Manganese in PDB 1qpr: Quinolinate Phosphoribosyltransferase (Qaprtase) From Mycobacterium Tuberculosis in Complex with Phthalate and Prpcp
Enzymatic activity of Quinolinate Phosphoribosyltransferase (Qaprtase) From Mycobacterium Tuberculosis in Complex with Phthalate and Prpcp
All present enzymatic activity of Quinolinate Phosphoribosyltransferase (Qaprtase) From Mycobacterium Tuberculosis in Complex with Phthalate and Prpcp:
2.4.2.19;
Protein crystallography data
The structure of Quinolinate Phosphoribosyltransferase (Qaprtase) From Mycobacterium Tuberculosis in Complex with Phthalate and Prpcp, PDB code: 1qpr
was solved by
V.Sharma,
C.Grubmeyer,
J.C.Sacchettini,
Tb Structural Genomicsconsortium (Tbsgc),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
8.00 /
2.45
|
Space group
|
P 31
|
Cell size a, b, c (Å), α, β, γ (°)
|
100.448,
100.448,
145.792,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
18.6 /
25.1
|
Manganese Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
12;
Binding sites:
The binding sites of Manganese atom in the Quinolinate Phosphoribosyltransferase (Qaprtase) From Mycobacterium Tuberculosis in Complex with Phthalate and Prpcp
(pdb code 1qpr). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 12 binding sites of Manganese where determined in the
Quinolinate Phosphoribosyltransferase (Qaprtase) From Mycobacterium Tuberculosis in Complex with Phthalate and Prpcp, PDB code: 1qpr:
Jump to Manganese binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Manganese binding site 1 out
of 12 in 1qpr
Go back to
Manganese Binding Sites List in 1qpr
Manganese binding site 1 out
of 12 in the Quinolinate Phosphoribosyltransferase (Qaprtase) From Mycobacterium Tuberculosis in Complex with Phthalate and Prpcp
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Quinolinate Phosphoribosyltransferase (Qaprtase) From Mycobacterium Tuberculosis in Complex with Phthalate and Prpcp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn286
b:79.7
occ:1.00
|
O
|
A:HOH3316
|
2.0
|
76.9
|
1.0
|
O
|
A:HOH3317
|
2.0
|
75.1
|
1.0
|
O
|
A:HOH3319
|
2.1
|
78.4
|
1.0
|
O1A
|
B:PPC288
|
2.1
|
77.2
|
1.0
|
O
|
B:HOH3318
|
2.2
|
74.9
|
1.0
|
O3B
|
B:PPC288
|
2.3
|
76.4
|
1.0
|
PA
|
B:PPC288
|
3.5
|
77.2
|
1.0
|
PB
|
B:PPC288
|
3.5
|
77.9
|
1.0
|
C3A
|
B:PPC288
|
3.8
|
77.7
|
1.0
|
OD2
|
A:ASP280
|
3.8
|
31.9
|
1.0
|
OD1
|
A:ASP280
|
3.9
|
30.5
|
1.0
|
NH1
|
A:ARG48
|
4.1
|
25.2
|
1.0
|
O4
|
B:PPC288
|
4.1
|
67.9
|
1.0
|
CG
|
A:ASP280
|
4.3
|
28.6
|
1.0
|
O1B
|
B:PPC288
|
4.3
|
77.6
|
1.0
|
NZ
|
B:LYS140
|
4.5
|
25.2
|
1.0
|
O2A
|
B:PPC288
|
4.5
|
76.9
|
1.0
|
CD
|
A:ARG48
|
4.6
|
19.1
|
1.0
|
O1P
|
B:PPC288
|
4.6
|
40.4
|
1.0
|
O1
|
B:PPC288
|
4.6
|
75.0
|
1.0
|
O3
|
B:PPC288
|
4.7
|
71.1
|
1.0
|
C4
|
B:PPC288
|
4.7
|
63.0
|
1.0
|
CG
|
A:ARG48
|
4.8
|
16.4
|
1.0
|
O2B
|
B:PPC288
|
4.9
|
80.1
|
1.0
|
|
Manganese binding site 2 out
of 12 in 1qpr
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Manganese Binding Sites List in 1qpr
Manganese binding site 2 out
of 12 in the Quinolinate Phosphoribosyltransferase (Qaprtase) From Mycobacterium Tuberculosis in Complex with Phthalate and Prpcp
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Quinolinate Phosphoribosyltransferase (Qaprtase) From Mycobacterium Tuberculosis in Complex with Phthalate and Prpcp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn287
b:85.8
occ:1.00
|
O
|
A:HOH3329
|
1.8
|
80.2
|
1.0
|
O1
|
A:PPC288
|
2.1
|
76.6
|
1.0
|
O
|
A:HOH3328
|
2.2
|
78.7
|
1.0
|
O2
|
A:PPC288
|
2.2
|
77.3
|
1.0
|
O1B
|
A:PPC288
|
2.3
|
79.0
|
1.0
|
O3
|
A:PPC288
|
2.3
|
73.4
|
1.0
|
C2
|
A:PPC288
|
2.6
|
71.5
|
1.0
|
C1
|
A:PPC288
|
2.8
|
70.8
|
1.0
|
C3
|
A:PPC288
|
3.0
|
68.9
|
1.0
|
OD1
|
A:ASP222
|
3.5
|
34.2
|
1.0
|
O4
|
A:PPC288
|
3.5
|
69.5
|
1.0
|
PA
|
A:PPC288
|
3.5
|
74.6
|
1.0
|
OE1
|
A:GLU201
|
3.6
|
41.0
|
1.0
|
PB
|
A:PPC288
|
3.7
|
81.6
|
1.0
|
OE2
|
A:GLU201
|
3.7
|
41.3
|
1.0
|
CD
|
A:GLU201
|
3.9
|
40.3
|
1.0
|
C4
|
A:PPC288
|
3.9
|
63.9
|
1.0
|
CG
|
A:ASP222
|
3.9
|
30.7
|
1.0
|
C3A
|
A:PPC288
|
3.9
|
78.9
|
1.0
|
OD2
|
A:ASP222
|
4.0
|
39.6
|
1.0
|
O1A
|
A:PPC288
|
4.1
|
75.0
|
1.0
|
O
|
A:HOH3005
|
4.2
|
30.9
|
1.0
|
O
|
A:HOH3306
|
4.6
|
74.8
|
1.0
|
O3B
|
A:PPC288
|
4.7
|
79.7
|
1.0
|
O2A
|
A:PPC288
|
4.8
|
77.6
|
1.0
|
O2B
|
A:PPC288
|
4.9
|
80.7
|
1.0
|
O
|
A:HOH3006
|
4.9
|
46.4
|
1.0
|
NZ
|
A:LYS172
|
4.9
|
20.9
|
1.0
|
CB
|
A:ASP222
|
4.9
|
24.9
|
1.0
|
CG
|
A:GLU201
|
5.0
|
33.2
|
1.0
|
|
Manganese binding site 3 out
of 12 in 1qpr
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Manganese Binding Sites List in 1qpr
Manganese binding site 3 out
of 12 in the Quinolinate Phosphoribosyltransferase (Qaprtase) From Mycobacterium Tuberculosis in Complex with Phthalate and Prpcp
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 3 of Quinolinate Phosphoribosyltransferase (Qaprtase) From Mycobacterium Tuberculosis in Complex with Phthalate and Prpcp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn286
b:77.5
occ:1.00
|
O
|
A:HOH3304
|
2.0
|
75.9
|
1.0
|
O
|
B:HOH3305
|
2.0
|
77.9
|
1.0
|
O1A
|
A:PPC288
|
2.0
|
75.0
|
1.0
|
O
|
B:HOH3307
|
2.1
|
77.0
|
1.0
|
O
|
A:HOH3306
|
2.1
|
74.8
|
1.0
|
O3B
|
A:PPC288
|
2.4
|
79.7
|
1.0
|
PA
|
A:PPC288
|
3.4
|
74.6
|
1.0
|
PB
|
A:PPC288
|
3.6
|
81.6
|
1.0
|
OD2
|
B:ASP280
|
3.6
|
26.1
|
1.0
|
OD1
|
B:ASP280
|
3.8
|
32.5
|
1.0
|
C3A
|
A:PPC288
|
3.8
|
78.9
|
1.0
|
O4
|
A:PPC288
|
4.0
|
69.5
|
1.0
|
CG
|
B:ASP280
|
4.1
|
27.4
|
1.0
|
O1B
|
A:PPC288
|
4.3
|
79.0
|
1.0
|
NZ
|
A:LYS140
|
4.4
|
23.9
|
1.0
|
O2A
|
A:PPC288
|
4.4
|
77.6
|
1.0
|
O1P
|
A:PPC288
|
4.5
|
39.5
|
1.0
|
O1
|
A:PPC288
|
4.5
|
76.6
|
1.0
|
O3
|
A:PPC288
|
4.5
|
73.4
|
1.0
|
C4
|
A:PPC288
|
4.6
|
63.9
|
1.0
|
NH1
|
B:ARG48
|
4.6
|
25.1
|
1.0
|
O
|
A:HOH3197
|
4.8
|
21.8
|
1.0
|
CD
|
B:ARG48
|
4.8
|
18.9
|
1.0
|
O2B
|
A:PPC288
|
5.0
|
80.7
|
1.0
|
C1
|
A:PPC288
|
5.0
|
70.8
|
1.0
|
|
Manganese binding site 4 out
of 12 in 1qpr
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Manganese Binding Sites List in 1qpr
Manganese binding site 4 out
of 12 in the Quinolinate Phosphoribosyltransferase (Qaprtase) From Mycobacterium Tuberculosis in Complex with Phthalate and Prpcp
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 4 of Quinolinate Phosphoribosyltransferase (Qaprtase) From Mycobacterium Tuberculosis in Complex with Phthalate and Prpcp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn287
b:82.7
occ:1.00
|
O
|
B:HOH3335
|
1.8
|
80.0
|
1.0
|
O
|
B:HOH3334
|
2.1
|
76.5
|
1.0
|
O2
|
B:PPC288
|
2.1
|
75.8
|
1.0
|
O1
|
B:PPC288
|
2.2
|
75.0
|
1.0
|
O3
|
B:PPC288
|
2.4
|
71.1
|
1.0
|
O1B
|
B:PPC288
|
2.4
|
77.6
|
1.0
|
C2
|
B:PPC288
|
2.6
|
71.3
|
1.0
|
C1
|
B:PPC288
|
2.8
|
70.7
|
1.0
|
C3
|
B:PPC288
|
2.9
|
68.0
|
1.0
|
O4
|
B:PPC288
|
3.5
|
67.9
|
1.0
|
PA
|
B:PPC288
|
3.6
|
77.2
|
1.0
|
OE1
|
B:GLU201
|
3.6
|
35.0
|
1.0
|
OD1
|
B:ASP222
|
3.6
|
39.2
|
1.0
|
PB
|
B:PPC288
|
3.8
|
77.9
|
1.0
|
OE2
|
B:GLU201
|
3.8
|
41.0
|
1.0
|
CD
|
B:GLU201
|
3.9
|
36.7
|
1.0
|
C4
|
B:PPC288
|
3.9
|
63.0
|
1.0
|
CG
|
B:ASP222
|
3.9
|
32.4
|
1.0
|
OD2
|
B:ASP222
|
3.9
|
37.9
|
1.0
|
C3A
|
B:PPC288
|
4.0
|
77.7
|
1.0
|
O1A
|
B:PPC288
|
4.2
|
77.2
|
1.0
|
O
|
B:HOH3318
|
4.6
|
74.9
|
1.0
|
NZ
|
B:LYS172
|
4.6
|
31.9
|
1.0
|
O3B
|
B:PPC288
|
4.8
|
76.4
|
1.0
|
O2A
|
B:PPC288
|
4.9
|
76.9
|
1.0
|
O2B
|
B:PPC288
|
4.9
|
80.1
|
1.0
|
CG
|
B:GLU201
|
4.9
|
32.3
|
1.0
|
CB
|
B:ASP222
|
4.9
|
25.3
|
1.0
|
|
Manganese binding site 5 out
of 12 in 1qpr
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Manganese Binding Sites List in 1qpr
Manganese binding site 5 out
of 12 in the Quinolinate Phosphoribosyltransferase (Qaprtase) From Mycobacterium Tuberculosis in Complex with Phthalate and Prpcp
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 5 of Quinolinate Phosphoribosyltransferase (Qaprtase) From Mycobacterium Tuberculosis in Complex with Phthalate and Prpcp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn286
b:84.0
occ:1.00
|
O
|
D:HOH3308
|
2.0
|
80.5
|
1.0
|
O
|
C:HOH3309
|
2.1
|
75.0
|
1.0
|
O
|
C:HOH3311
|
2.1
|
77.0
|
1.0
|
O
|
D:HOH3310
|
2.1
|
76.0
|
1.0
|
O1A
|
D:PPC288
|
2.1
|
78.9
|
1.0
|
O3B
|
D:PPC288
|
2.5
|
79.6
|
1.0
|
PA
|
D:PPC288
|
3.5
|
76.0
|
1.0
|
PB
|
D:PPC288
|
3.6
|
82.8
|
1.0
|
C3A
|
D:PPC288
|
3.8
|
79.1
|
1.0
|
OD2
|
C:ASP280
|
3.8
|
29.1
|
1.0
|
O
|
D:HOH3035
|
4.0
|
36.6
|
1.0
|
OD1
|
C:ASP280
|
4.1
|
26.2
|
1.0
|
O4
|
D:PPC288
|
4.1
|
67.6
|
1.0
|
O1B
|
D:PPC288
|
4.3
|
77.2
|
1.0
|
NZ
|
D:LYS140
|
4.4
|
23.3
|
1.0
|
CG
|
C:ASP280
|
4.4
|
25.5
|
1.0
|
NH1
|
C:ARG48
|
4.5
|
27.1
|
1.0
|
O1P
|
D:PPC288
|
4.5
|
42.6
|
1.0
|
O2A
|
D:PPC288
|
4.5
|
77.5
|
1.0
|
O1
|
D:PPC288
|
4.6
|
74.4
|
1.0
|
O3
|
D:PPC288
|
4.7
|
72.4
|
1.0
|
C4
|
D:PPC288
|
4.7
|
62.0
|
1.0
|
CD
|
C:ARG48
|
4.8
|
18.6
|
1.0
|
CG
|
C:ARG48
|
5.0
|
22.2
|
1.0
|
|
Manganese binding site 6 out
of 12 in 1qpr
Go back to
Manganese Binding Sites List in 1qpr
Manganese binding site 6 out
of 12 in the Quinolinate Phosphoribosyltransferase (Qaprtase) From Mycobacterium Tuberculosis in Complex with Phthalate and Prpcp
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 6 of Quinolinate Phosphoribosyltransferase (Qaprtase) From Mycobacterium Tuberculosis in Complex with Phthalate and Prpcp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn287
b:84.1
occ:1.00
|
O
|
C:HOH3333
|
2.0
|
81.9
|
1.0
|
O
|
C:HOH3332
|
2.1
|
78.8
|
1.0
|
O1
|
C:PPC288
|
2.1
|
75.8
|
1.0
|
O2
|
C:PPC288
|
2.1
|
77.2
|
1.0
|
O1B
|
C:PPC288
|
2.3
|
79.6
|
1.0
|
O3
|
C:PPC288
|
2.4
|
73.1
|
1.0
|
C2
|
C:PPC288
|
2.5
|
72.0
|
1.0
|
C1
|
C:PPC288
|
2.7
|
71.1
|
1.0
|
C3
|
C:PPC288
|
2.9
|
69.3
|
1.0
|
O4
|
C:PPC288
|
3.5
|
68.1
|
1.0
|
OE1
|
C:GLU201
|
3.5
|
39.3
|
1.0
|
PA
|
C:PPC288
|
3.5
|
75.7
|
1.0
|
OD1
|
C:ASP222
|
3.6
|
30.1
|
1.0
|
PB
|
C:PPC288
|
3.7
|
85.3
|
1.0
|
CD
|
C:GLU201
|
3.8
|
35.2
|
1.0
|
C4
|
C:PPC288
|
3.8
|
63.2
|
1.0
|
OE2
|
C:GLU201
|
3.9
|
37.5
|
1.0
|
C3A
|
C:PPC288
|
4.0
|
80.4
|
1.0
|
CG
|
C:ASP222
|
4.0
|
24.3
|
1.0
|
O1A
|
C:PPC288
|
4.1
|
79.8
|
1.0
|
OD2
|
C:ASP222
|
4.2
|
32.4
|
1.0
|
O
|
C:HOH3314
|
4.6
|
77.3
|
1.0
|
O3B
|
C:PPC288
|
4.7
|
81.6
|
1.0
|
NZ
|
C:LYS172
|
4.7
|
25.1
|
1.0
|
CD2
|
C:LEU220
|
4.8
|
21.8
|
1.0
|
O2A
|
C:PPC288
|
4.8
|
76.3
|
1.0
|
CG
|
C:GLU201
|
4.9
|
27.9
|
1.0
|
O2B
|
C:PPC288
|
4.9
|
83.5
|
1.0
|
CB
|
C:ASP222
|
4.9
|
19.5
|
1.0
|
|
Manganese binding site 7 out
of 12 in 1qpr
Go back to
Manganese Binding Sites List in 1qpr
Manganese binding site 7 out
of 12 in the Quinolinate Phosphoribosyltransferase (Qaprtase) From Mycobacterium Tuberculosis in Complex with Phthalate and Prpcp
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 7 of Quinolinate Phosphoribosyltransferase (Qaprtase) From Mycobacterium Tuberculosis in Complex with Phthalate and Prpcp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mn286
b:87.8
occ:1.00
|
O
|
C:HOH3312
|
2.0
|
79.2
|
1.0
|
O1A
|
C:PPC288
|
2.1
|
79.8
|
1.0
|
O
|
C:HOH3315
|
2.1
|
80.2
|
1.0
|
O
|
D:HOH3313
|
2.2
|
78.1
|
1.0
|
O
|
C:HOH3314
|
2.2
|
77.3
|
1.0
|
O3B
|
C:PPC288
|
2.4
|
81.6
|
1.0
|
PA
|
C:PPC288
|
3.5
|
75.7
|
1.0
|
PB
|
C:PPC288
|
3.5
|
85.3
|
1.0
|
C3A
|
C:PPC288
|
3.7
|
80.4
|
1.0
|
OD2
|
D:ASP280
|
3.9
|
31.9
|
1.0
|
O4
|
C:PPC288
|
4.0
|
68.1
|
1.0
|
OD1
|
D:ASP280
|
4.1
|
37.9
|
1.0
|
O1B
|
C:PPC288
|
4.3
|
79.6
|
1.0
|
CG
|
D:ASP280
|
4.5
|
31.0
|
1.0
|
O2A
|
C:PPC288
|
4.5
|
76.3
|
1.0
|
O1P
|
C:PPC288
|
4.5
|
37.3
|
1.0
|
O3
|
C:PPC288
|
4.5
|
73.1
|
1.0
|
O1
|
C:PPC288
|
4.5
|
75.8
|
1.0
|
C4
|
C:PPC288
|
4.6
|
63.2
|
1.0
|
NZ
|
C:LYS140
|
4.6
|
21.8
|
1.0
|
ND2
|
C:ASN223
|
4.7
|
45.7
|
1.0
|
NH1
|
D:ARG48
|
4.8
|
33.7
|
1.0
|
C1
|
C:PPC288
|
5.0
|
71.1
|
1.0
|
O2B
|
C:PPC288
|
5.0
|
83.5
|
1.0
|
|
Manganese binding site 8 out
of 12 in 1qpr
Go back to
Manganese Binding Sites List in 1qpr
Manganese binding site 8 out
of 12 in the Quinolinate Phosphoribosyltransferase (Qaprtase) From Mycobacterium Tuberculosis in Complex with Phthalate and Prpcp
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 8 of Quinolinate Phosphoribosyltransferase (Qaprtase) From Mycobacterium Tuberculosis in Complex with Phthalate and Prpcp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mn287
b:83.4
occ:1.00
|
O
|
D:HOH3331
|
1.8
|
80.0
|
1.0
|
O2
|
D:PPC288
|
2.1
|
76.6
|
1.0
|
O1
|
D:PPC288
|
2.1
|
74.4
|
1.0
|
O
|
D:HOH3330
|
2.1
|
77.1
|
1.0
|
O3
|
D:PPC288
|
2.3
|
72.4
|
1.0
|
O1B
|
D:PPC288
|
2.3
|
77.2
|
1.0
|
C2
|
D:PPC288
|
2.5
|
70.9
|
1.0
|
C1
|
D:PPC288
|
2.7
|
70.2
|
1.0
|
C3
|
D:PPC288
|
2.9
|
68.8
|
1.0
|
OD1
|
D:ASP222
|
3.4
|
33.0
|
1.0
|
O4
|
D:PPC288
|
3.5
|
67.6
|
1.0
|
OE1
|
D:GLU201
|
3.6
|
35.2
|
1.0
|
PA
|
D:PPC288
|
3.6
|
76.0
|
1.0
|
PB
|
D:PPC288
|
3.7
|
82.8
|
1.0
|
CG
|
D:ASP222
|
3.8
|
32.4
|
1.0
|
C4
|
D:PPC288
|
3.8
|
62.0
|
1.0
|
C3A
|
D:PPC288
|
4.0
|
79.1
|
1.0
|
O
|
D:HOH3087
|
4.0
|
26.1
|
1.0
|
OD2
|
D:ASP222
|
4.0
|
38.3
|
1.0
|
CD
|
D:GLU201
|
4.0
|
37.3
|
1.0
|
OE2
|
D:GLU201
|
4.1
|
39.6
|
1.0
|
O1A
|
D:PPC288
|
4.2
|
78.9
|
1.0
|
O
|
D:HOH3081
|
4.3
|
36.6
|
1.0
|
O
|
D:HOH3310
|
4.6
|
76.0
|
1.0
|
NZ
|
D:LYS172
|
4.6
|
25.9
|
1.0
|
CB
|
D:ASP222
|
4.7
|
22.9
|
1.0
|
O3B
|
D:PPC288
|
4.8
|
79.6
|
1.0
|
CD2
|
D:LEU220
|
4.8
|
19.6
|
1.0
|
O
|
D:HOH3086
|
4.9
|
30.4
|
1.0
|
O2B
|
D:PPC288
|
4.9
|
82.9
|
1.0
|
O2A
|
D:PPC288
|
4.9
|
77.5
|
1.0
|
|
Manganese binding site 9 out
of 12 in 1qpr
Go back to
Manganese Binding Sites List in 1qpr
Manganese binding site 9 out
of 12 in the Quinolinate Phosphoribosyltransferase (Qaprtase) From Mycobacterium Tuberculosis in Complex with Phthalate and Prpcp
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 9 of Quinolinate Phosphoribosyltransferase (Qaprtase) From Mycobacterium Tuberculosis in Complex with Phthalate and Prpcp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mn286
b:75.1
occ:1.00
|
O
|
F:HOH3324
|
2.0
|
75.4
|
1.0
|
O
|
F:HOH3325
|
2.1
|
74.3
|
1.0
|
O1A
|
F:PPC288
|
2.1
|
76.0
|
1.0
|
O
|
F:HOH3326
|
2.1
|
70.8
|
1.0
|
O
|
F:HOH3327
|
2.2
|
76.1
|
1.0
|
O3B
|
F:PPC288
|
2.3
|
78.3
|
1.0
|
PA
|
F:PPC288
|
3.5
|
68.6
|
1.0
|
PB
|
F:PPC288
|
3.5
|
81.7
|
1.0
|
C3A
|
F:PPC288
|
3.7
|
76.0
|
1.0
|
O4
|
F:PPC288
|
4.0
|
63.7
|
1.0
|
OD2
|
E:ASP280
|
4.0
|
24.4
|
1.0
|
OD1
|
E:ASP280
|
4.2
|
30.0
|
1.0
|
O1B
|
F:PPC288
|
4.2
|
77.1
|
1.0
|
NH1
|
E:ARG48
|
4.3
|
28.9
|
1.0
|
O2A
|
F:PPC288
|
4.5
|
71.2
|
1.0
|
CG
|
E:ASP280
|
4.5
|
23.9
|
1.0
|
O1
|
F:PPC288
|
4.5
|
71.7
|
1.0
|
NZ
|
F:LYS140
|
4.5
|
14.4
|
1.0
|
O3
|
F:PPC288
|
4.5
|
69.7
|
1.0
|
O1P
|
F:PPC288
|
4.5
|
30.3
|
1.0
|
C4
|
F:PPC288
|
4.6
|
59.9
|
1.0
|
O
|
F:HOH3104
|
4.9
|
14.7
|
1.0
|
O2B
|
F:PPC288
|
4.9
|
82.8
|
1.0
|
C1
|
F:PPC288
|
5.0
|
66.9
|
1.0
|
|
Manganese binding site 10 out
of 12 in 1qpr
Go back to
Manganese Binding Sites List in 1qpr
Manganese binding site 10 out
of 12 in the Quinolinate Phosphoribosyltransferase (Qaprtase) From Mycobacterium Tuberculosis in Complex with Phthalate and Prpcp
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 10 of Quinolinate Phosphoribosyltransferase (Qaprtase) From Mycobacterium Tuberculosis in Complex with Phthalate and Prpcp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mn287
b:82.1
occ:1.00
|
O
|
E:HOH3337
|
1.9
|
78.9
|
1.0
|
O2
|
E:PPC288
|
2.1
|
77.7
|
1.0
|
O
|
E:HOH3336
|
2.1
|
77.6
|
1.0
|
O1
|
E:PPC288
|
2.2
|
76.6
|
1.0
|
O1B
|
E:PPC288
|
2.3
|
78.5
|
1.0
|
O3
|
E:PPC288
|
2.4
|
72.3
|
1.0
|
C2
|
E:PPC288
|
2.5
|
72.7
|
1.0
|
C1
|
E:PPC288
|
2.8
|
72.5
|
1.0
|
C3
|
E:PPC288
|
2.9
|
69.5
|
1.0
|
OE1
|
E:GLU201
|
3.4
|
36.0
|
1.0
|
O4
|
E:PPC288
|
3.5
|
69.9
|
1.0
|
PA
|
E:PPC288
|
3.6
|
81.5
|
1.0
|
PB
|
E:PPC288
|
3.7
|
85.8
|
1.0
|
OD1
|
E:ASP222
|
3.7
|
30.5
|
1.0
|
OE2
|
E:GLU201
|
3.8
|
43.0
|
1.0
|
CD
|
E:GLU201
|
3.8
|
36.1
|
1.0
|
C4
|
E:PPC288
|
3.9
|
64.2
|
1.0
|
C3A
|
E:PPC288
|
4.0
|
81.4
|
1.0
|
O1A
|
E:PPC288
|
4.2
|
80.5
|
1.0
|
CG
|
E:ASP222
|
4.2
|
29.8
|
1.0
|
NZ
|
E:LYS172
|
4.3
|
20.1
|
1.0
|
OD2
|
E:ASP222
|
4.5
|
36.0
|
1.0
|
O
|
E:HOH3322
|
4.6
|
78.8
|
1.0
|
O3B
|
E:PPC288
|
4.7
|
83.0
|
1.0
|
CD2
|
E:LEU220
|
4.7
|
20.4
|
1.0
|
O11
|
E:PHT1
|
4.8
|
21.9
|
1.0
|
O2B
|
E:PPC288
|
4.8
|
84.4
|
1.0
|
CG
|
E:GLU201
|
4.9
|
33.7
|
1.0
|
O2A
|
E:PPC288
|
4.9
|
80.1
|
1.0
|
|
Reference:
V.Sharma,
C.Grubmeyer,
J.C.Sacchettini.
Crystal Structure of Quinolinic Acid Phosphoribosyltransferase From Mycobacterium Tuberculosis: A Potential Tb Drug Target. Structure V. 6 1587 1998.
ISSN: ISSN 0969-2126
PubMed: 9862811
DOI: 10.1016/S0969-2126(98)00156-7
Page generated: Sat Oct 5 12:15:11 2024
|