Atomistry » Manganese » PDB 1pj4-1r1o » 1qpr
Atomistry »
  Manganese »
    PDB 1pj4-1r1o »
      1qpr »

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

Go back to 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

Go back to 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

Go back to 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

Go back to 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

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy