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Magnesium in PDB 3ldw: Crystal Structure of Plasmodium Vivax Geranylgeranylpyrophosphate Synthase PVX_092040 with Zoledronate and Ipp Bound

Protein crystallography data

The structure of Crystal Structure of Plasmodium Vivax Geranylgeranylpyrophosphate Synthase PVX_092040 with Zoledronate and Ipp Bound, PDB code: 3ldw was solved by A.K.Wernimont, J.Lew, Y.Zhao, I.Kozieradzki, D.Cossar, M.Schapira, A.Bochkarev, C.H.Arrowsmith, C.Bountra, J.Weigelt, A.M.Edwards, R.Hui, J.D.Artz, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.24 / 2.47
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 111.264, 139.543, 109.711, 90.00, 90.00, 90.00
R / Rfree (%) 23.9 / 28.6

Magnesium Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Magnesium atom in the Crystal Structure of Plasmodium Vivax Geranylgeranylpyrophosphate Synthase PVX_092040 with Zoledronate and Ipp Bound (pdb code 3ldw). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 12 binding sites of Magnesium where determined in the Crystal Structure of Plasmodium Vivax Geranylgeranylpyrophosphate Synthase PVX_092040 with Zoledronate and Ipp Bound, PDB code: 3ldw:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Magnesium binding site 1 out of 12 in 3ldw

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Magnesium binding site 1 out of 12 in the Crystal Structure of Plasmodium Vivax Geranylgeranylpyrophosphate Synthase PVX_092040 with Zoledronate and Ipp Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Plasmodium Vivax Geranylgeranylpyrophosphate Synthase PVX_092040 with Zoledronate and Ipp Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1102

b:21.6
occ:1.00
O17 A:ZOL397 2.0 43.9 1.0
OD2 A:ASP130 2.0 36.7 1.0
OD2 A:ASP126 2.1 22.2 1.0
O12 A:ZOL397 2.1 20.3 1.0
O A:HOH1164 2.2 27.4 1.0
O A:HOH1142 2.4 22.2 1.0
OD1 A:ASP126 2.6 21.0 1.0
CG A:ASP126 2.7 22.8 1.0
MG A:MG1103 3.0 22.8 1.0
CG A:ASP130 3.1 30.6 1.0
P14 A:ZOL397 3.2 30.7 1.0
P9 A:ZOL397 3.4 30.7 1.0
C8 A:ZOL397 3.6 15.1 1.0
CB A:ASP130 3.7 23.0 1.0
C7 A:ZOL397 3.9 20.0 1.0
O11 A:ZOL397 4.0 21.5 1.0
O A:HOH1162 4.0 38.1 1.0
O16 A:ZOL397 4.1 22.8 1.0
CB A:ASP126 4.1 22.9 1.0
OD1 A:ASP130 4.2 29.9 1.0
O A:ASP126 4.2 21.6 1.0
O A:HOH1155 4.2 37.7 1.0
O A:HOH1161 4.4 50.1 1.0
O15 A:ZOL397 4.4 17.1 1.0
C A:ASP126 4.5 23.0 1.0
NH1 A:ARG135 4.5 11.5 1.0
OD1 A:ASP127 4.5 19.0 1.0
O10 A:ZOL397 4.6 37.5 1.0
O A:HOH1154 4.7 39.3 1.0
O A:HOH1130 4.7 23.1 1.0
O A:HOH1251 4.8 15.2 1.0
CA A:ASP126 4.8 21.6 1.0
N15 A:ZOL397 4.9 30.3 1.0
O A:HOH1132 4.9 25.2 1.0

Magnesium binding site 2 out of 12 in 3ldw

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Magnesium binding site 2 out of 12 in the Crystal Structure of Plasmodium Vivax Geranylgeranylpyrophosphate Synthase PVX_092040 with Zoledronate and Ipp Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Plasmodium Vivax Geranylgeranylpyrophosphate Synthase PVX_092040 with Zoledronate and Ipp Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1103

b:22.8
occ:1.00
OD1 A:ASP126 2.0 21.0 1.0
O A:HOH1162 2.0 38.1 1.0
OD2 A:ASP130 2.1 36.7 1.0
O A:HOH1161 2.2 50.1 1.0
O12 A:ZOL397 2.2 20.3 1.0
O A:HOH1143 2.4 20.6 1.0
O A:HOH1130 2.4 23.1 1.0
CG A:ASP130 2.8 30.6 1.0
OD1 A:ASP130 2.8 29.9 1.0
MG A:MG1102 3.0 21.6 1.0
CG A:ASP126 3.2 22.8 1.0
P9 A:ZOL397 3.6 30.7 1.0
OD2 A:ASP198 3.8 44.6 1.0
OD2 A:ASP126 3.8 22.2 1.0
O10 A:ZOL397 3.9 37.5 1.0
NE2 A:GLN195 4.1 30.5 1.0
O A:HOH1164 4.2 27.4 1.0
CB A:ASP130 4.2 23.0 1.0
OE1 A:GLN195 4.3 27.9 1.0
CB A:ASP126 4.3 22.9 1.0
CG A:ASP198 4.4 30.4 1.0
O A:ASP126 4.4 21.6 1.0
OD1 A:ASP198 4.5 29.3 1.0
C19 A:ZOL397 4.5 21.6 1.0
NZ A:LYS310 4.6 31.8 1.0
CD A:GLN195 4.6 33.4 1.0
O11 A:ZOL397 4.7 21.5 1.0
C7 A:ZOL397 4.7 20.0 1.0
CA A:ASP126 4.7 21.6 1.0
C8 A:ZOL397 4.7 15.1 1.0
O17 A:ZOL397 4.7 43.9 1.0
N15 A:ZOL397 4.8 30.3 1.0
CE A:LYS310 4.8 29.1 1.0
C A:ASP126 4.9 23.0 1.0
O A:HOH1117 4.9 17.6 1.0

Magnesium binding site 3 out of 12 in 3ldw

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Magnesium binding site 3 out of 12 in the Crystal Structure of Plasmodium Vivax Geranylgeranylpyrophosphate Synthase PVX_092040 with Zoledronate and Ipp Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Plasmodium Vivax Geranylgeranylpyrophosphate Synthase PVX_092040 with Zoledronate and Ipp Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1104

b:23.6
occ:1.00
O A:HOH1144 2.0 16.4 1.0
O11 A:ZOL397 2.0 21.5 1.0
O16 A:ZOL397 2.0 22.8 1.0
O A:HOH1116 2.1 19.0 1.0
O A:HOH1251 2.4 15.2 1.0
OD1 A:ASP287 2.4 26.7 1.0
CG A:ASP287 3.3 28.7 1.0
P14 A:ZOL397 3.4 30.7 1.0
P9 A:ZOL397 3.5 30.7 1.0
O A:HOH1117 3.5 17.6 1.0
OD2 A:ASP287 3.6 31.3 1.0
O13 A:ZOL397 3.7 20.3 1.0
C8 A:ZOL397 3.8 15.1 1.0
OD1 A:ASP305 3.9 34.6 1.0
O A:HOH1164 3.9 27.4 1.0
OD2 A:ASP305 4.0 39.2 1.0
O A:HOH1246 4.1 42.4 1.0
O17 A:ZOL397 4.2 43.9 1.0
O12 A:ZOL397 4.3 20.3 1.0
O A:ASP287 4.4 32.0 1.0
CG A:ASP305 4.4 34.6 1.0
OD2 A:ASP288 4.4 29.5 1.0
NE2 A:GLN284 4.4 28.9 1.0
OD2 A:ASP291 4.4 42.6 1.0
O10 A:ZOL397 4.4 37.5 1.0
O15 A:ZOL397 4.5 17.1 1.0
CB A:ASP287 4.5 27.4 1.0
C A:ASP287 4.5 31.4 1.0
CB A:ASP291 4.6 29.6 1.0
NZ A:LYS301 4.8 28.7 1.0
CG A:ASP291 4.9 36.9 1.0
N A:ASP288 4.9 26.3 1.0
CE A:LYS301 4.9 28.6 1.0

Magnesium binding site 4 out of 12 in 3ldw

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Magnesium binding site 4 out of 12 in the Crystal Structure of Plasmodium Vivax Geranylgeranylpyrophosphate Synthase PVX_092040 with Zoledronate and Ipp Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of Plasmodium Vivax Geranylgeranylpyrophosphate Synthase PVX_092040 with Zoledronate and Ipp Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1102

b:21.8
occ:1.00
O B:HOH1144 1.9 16.6 1.0
OD2 B:ASP130 2.1 28.1 1.0
O B:HOH1145 2.1 15.8 1.0
O12 B:ZOL397 2.2 24.6 1.0
OD2 B:ASP126 2.3 25.8 1.0
O B:HOH1186 2.3 23.8 1.0
CG B:ASP130 2.8 22.1 1.0
OD1 B:ASP130 2.8 18.1 1.0
CG B:ASP126 3.2 22.6 1.0
MG B:MG1104 3.4 15.9 1.0
P9 B:ZOL397 3.4 23.4 1.0
O10 B:ZOL397 3.5 31.4 1.0
OD1 B:ASP126 3.5 20.6 1.0
OD2 B:ASP198 3.6 41.9 1.0
O B:HOH1187 4.1 19.9 1.0
OD1 B:ASP198 4.1 34.5 1.0
CG B:ASP198 4.2 34.9 1.0
CB B:ASP130 4.2 21.1 1.0
OE1 B:GLN195 4.4 26.0 1.0
NZ B:LYS310 4.4 24.8 1.0
NE2 B:GLN195 4.4 14.4 1.0
O11 B:ZOL397 4.4 11.2 1.0
CB B:ASP126 4.5 20.3 1.0
O B:HOH1261 4.6 20.0 1.0
CE B:LYS310 4.6 16.0 1.0
O B:ASP126 4.7 26.2 1.0
C19 B:ZOL397 4.8 29.8 1.0
O17 B:ZOL397 4.8 27.1 1.0
C8 B:ZOL397 4.8 11.1 1.0
CD B:GLN195 4.8 25.7 1.0
C7 B:ZOL397 4.9 27.8 1.0
N15 B:ZOL397 4.9 22.2 1.0
NZ B:LYS243 5.0 23.6 1.0
CA B:ASP126 5.0 19.4 1.0

Magnesium binding site 5 out of 12 in 3ldw

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Magnesium binding site 5 out of 12 in the Crystal Structure of Plasmodium Vivax Geranylgeranylpyrophosphate Synthase PVX_092040 with Zoledronate and Ipp Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Crystal Structure of Plasmodium Vivax Geranylgeranylpyrophosphate Synthase PVX_092040 with Zoledronate and Ipp Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1103

b:16.4
occ:1.00
O16 B:ZOL397 1.9 18.7 1.0
O B:HOH1149 2.0 27.6 1.0
O B:HOH1135 2.1 34.3 1.0
O11 B:ZOL397 2.2 11.2 1.0
OD1 B:ASP287 2.2 24.2 1.0
O B:HOH1164 2.3 21.7 1.0
CG B:ASP287 3.1 26.2 1.0
P14 B:ZOL397 3.4 24.9 1.0
OD2 B:ASP287 3.4 30.9 1.0
P9 B:ZOL397 3.6 23.4 1.0
O13 B:ZOL397 3.6 50.1 1.0
O B:HOH1261 3.7 20.0 1.0
C8 B:ZOL397 3.7 11.1 1.0
C1 B:EDO1106 3.9 38.8 1.0
OD2 B:ASP305 4.1 27.9 1.0
O B:ASP287 4.1 20.7 1.0
O2 B:EDO1106 4.2 38.2 1.0
O17 B:ZOL397 4.3 27.1 1.0
OD2 B:ASP291 4.3 43.2 1.0
C B:ASP287 4.3 22.9 1.0
CB B:ASP287 4.4 20.9 1.0
NE2 B:GLN284 4.4 15.3 1.0
O12 B:ZOL397 4.4 24.6 1.0
O B:HOH1187 4.4 19.9 1.0
CB B:ASP291 4.4 29.8 1.0
OD1 B:ASP305 4.5 30.6 1.0
O15 B:ZOL397 4.5 24.1 1.0
O10 B:ZOL397 4.6 31.4 1.0
OD2 B:ASP288 4.6 26.2 1.0
C2 B:EDO1106 4.6 37.3 1.0
CG B:ASP305 4.7 27.7 1.0
N B:ASP288 4.7 20.6 1.0
NZ B:LYS301 4.7 23.7 1.0
CG B:ASP291 4.7 35.1 1.0
O1 B:EDO1106 4.8 39.1 1.0
CE B:LYS301 4.9 23.0 1.0
CA B:ASP287 4.9 20.2 1.0
CA B:ASP288 5.0 20.5 1.0

Magnesium binding site 6 out of 12 in 3ldw

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Magnesium binding site 6 out of 12 in the Crystal Structure of Plasmodium Vivax Geranylgeranylpyrophosphate Synthase PVX_092040 with Zoledronate and Ipp Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of Crystal Structure of Plasmodium Vivax Geranylgeranylpyrophosphate Synthase PVX_092040 with Zoledronate and Ipp Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1104

b:15.9
occ:1.00
OD2 B:ASP130 2.0 28.1 1.0
O17 B:ZOL397 2.0 27.1 1.0
O B:HOH1187 2.0 19.9 1.0
OD1 B:ASP126 2.2 20.6 1.0
O12 B:ZOL397 2.2 24.6 1.0
O B:HOH1162 2.4 15.4 1.0
CG B:ASP130 3.0 22.1 1.0
CG B:ASP126 3.2 22.6 1.0
P14 B:ZOL397 3.3 24.9 1.0
MG B:MG1102 3.4 21.8 1.0
CB B:ASP130 3.4 21.1 1.0
OD2 B:ASP126 3.5 25.8 1.0
P9 B:ZOL397 3.6 23.4 1.0
C8 B:ZOL397 4.0 11.1 1.0
O B:HOH1138 4.0 25.9 1.0
O1 B:EDO1106 4.0 39.1 1.0
O11 B:ZOL397 4.0 11.2 1.0
O16 B:ZOL397 4.0 18.7 1.0
OD1 B:ASP130 4.2 18.1 1.0
NH2 B:ARG135 4.2 15.8 1.0
O B:HOH1164 4.3 21.7 1.0
C7 B:ZOL397 4.3 27.8 1.0
C1 B:EDO1106 4.4 38.8 1.0
O B:ASP126 4.4 26.2 1.0
O B:HOH1186 4.4 23.8 1.0
OD1 B:ASP127 4.5 25.5 1.0
CB B:ASP126 4.5 20.3 1.0
O15 B:ZOL397 4.5 24.1 1.0
O B:HOH1219 4.5 16.0 1.0
C B:ASP126 4.7 24.6 1.0
O10 B:ZOL397 4.8 31.4 1.0
O B:HOH1144 4.8 16.6 1.0
CA B:ASP130 4.9 20.4 1.0
O B:HOH1188 4.9 21.0 1.0

Magnesium binding site 7 out of 12 in 3ldw

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Magnesium binding site 7 out of 12 in the Crystal Structure of Plasmodium Vivax Geranylgeranylpyrophosphate Synthase PVX_092040 with Zoledronate and Ipp Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 7 of Crystal Structure of Plasmodium Vivax Geranylgeranylpyrophosphate Synthase PVX_092040 with Zoledronate and Ipp Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg1102

b:23.4
occ:1.00
O17 C:ZOL397 1.9 45.8 1.0
O C:HOH1192 2.1 25.7 1.0
OD1 C:ASP126 2.2 18.9 1.0
O12 C:ZOL397 2.2 27.1 1.0
O C:HOH1118 2.3 30.6 1.0
OD2 C:ASP130 2.5 36.7 1.0
P14 C:ZOL397 3.1 26.7 1.0
CG C:ASP126 3.2 21.5 1.0
MG C:MG1103 3.4 27.2 1.0
CG C:ASP130 3.4 28.4 1.0
OD2 C:ASP126 3.5 28.6 1.0
P9 C:ZOL397 3.5 23.7 1.0
CB C:ASP130 3.6 20.3 1.0
O16 C:ZOL397 3.8 17.0 1.0
C8 C:ZOL397 3.9 14.8 1.0
O C:HOH1212 3.9 38.7 1.0
O11 C:ZOL397 4.0 12.0 1.0
C7 C:ZOL397 4.2 20.6 1.0
O C:HOH1110 4.3 19.3 1.0
O C:HOH1120 4.3 4.3 0.5
OD1 C:ASP127 4.4 21.8 1.0
O C:ASP126 4.4 25.3 1.0
NH1 C:ARG135 4.4 20.8 1.0
O15 C:ZOL397 4.4 21.6 1.0
CB C:ASP126 4.5 19.5 1.0
O C:HOH1238 4.5 22.6 1.0
O C:HOH1142 4.5 36.3 1.0
OD1 C:ASP130 4.6 27.2 1.0
C C:ASP126 4.7 24.1 1.0
O10 C:ZOL397 4.7 38.8 1.0

Magnesium binding site 8 out of 12 in 3ldw

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Magnesium binding site 8 out of 12 in the Crystal Structure of Plasmodium Vivax Geranylgeranylpyrophosphate Synthase PVX_092040 with Zoledronate and Ipp Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 8 of Crystal Structure of Plasmodium Vivax Geranylgeranylpyrophosphate Synthase PVX_092040 with Zoledronate and Ipp Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg1103

b:27.2
occ:1.00
OD2 C:ASP130 1.9 36.7 1.0
O C:HOH1120 2.0 4.3 0.5
O C:HOH1175 2.1 13.4 1.0
O12 C:ZOL397 2.1 27.1 1.0
OD2 C:ASP126 2.2 28.6 1.0
O C:HOH1122 2.2 29.6 1.0
CG C:ASP130 2.9 28.4 1.0
CG C:ASP126 3.1 21.5 1.0
OD1 C:ASP130 3.2 27.2 1.0
P9 C:ZOL397 3.3 23.7 1.0
O10 C:ZOL397 3.4 38.8 1.0
MG C:MG1102 3.4 23.4 1.0
OD1 C:ASP126 3.5 18.9 1.0
OD2 C:ASP198 3.7 41.5 1.0
NE2 C:GLN195 4.2 27.4 1.0
O C:HOH1192 4.2 25.7 1.0
CG C:ASP198 4.2 33.2 1.0
OE1 C:GLN195 4.2 24.2 1.0
CB C:ASP130 4.2 20.3 1.0
OD1 C:ASP198 4.3 31.2 1.0
O11 C:ZOL397 4.4 12.0 1.0
CB C:ASP126 4.5 19.5 1.0
NZ C:LYS310 4.5 34.8 1.0
O C:HOH1176 4.6 20.4 1.0
C7 C:ZOL397 4.6 20.6 1.0
C19 C:ZOL397 4.6 7.1 1.0
C8 C:ZOL397 4.6 14.8 1.0
CD C:GLN195 4.6 28.2 1.0
O17 C:ZOL397 4.7 45.8 1.0
O C:ASP126 4.7 25.3 1.0
N15 C:ZOL397 4.7 25.6 1.0
CE C:LYS310 4.8 27.1 1.0
NZ C:LYS243 4.9 29.4 1.0
CA C:ASP126 5.0 18.7 1.0

Magnesium binding site 9 out of 12 in 3ldw

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Magnesium binding site 9 out of 12 in the Crystal Structure of Plasmodium Vivax Geranylgeranylpyrophosphate Synthase PVX_092040 with Zoledronate and Ipp Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 9 of Crystal Structure of Plasmodium Vivax Geranylgeranylpyrophosphate Synthase PVX_092040 with Zoledronate and Ipp Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg1104

b:27.3
occ:1.00
O C:HOH1191 1.9 30.4 1.0
O C:HOH1167 2.0 54.3 1.0
O16 C:ZOL397 2.1 17.0 1.0
O11 C:ZOL397 2.2 12.0 1.0
OD1 C:ASP287 2.3 32.3 1.0
O C:HOH1110 2.3 19.3 1.0
CG C:ASP287 3.2 32.4 1.0
OD2 C:ASP287 3.4 29.4 1.0
P14 C:ZOL397 3.6 26.7 1.0
P9 C:ZOL397 3.6 23.7 1.0
O C:HOH1176 3.7 20.4 1.0
O13 C:ZOL397 3.8 32.5 1.0
C8 C:ZOL397 3.9 14.8 1.0
OD2 C:ASP305 4.0 38.3 1.0
O C:ASP287 4.1 25.5 1.0
O C:HOH1192 4.2 25.7 1.0
OD1 C:ASP305 4.2 34.7 1.0
OD2 C:ASP291 4.2 46.8 1.0
C C:ASP287 4.3 28.2 1.0
CB C:ASP291 4.4 30.2 1.0
CB C:ASP287 4.4 24.9 1.0
NE2 C:GLN284 4.4 27.8 1.0
O12 C:ZOL397 4.4 27.1 1.0
O15 C:ZOL397 4.5 21.6 1.0
CG C:ASP305 4.5 33.5 1.0
OD2 C:ASP288 4.5 37.9 1.0
O17 C:ZOL397 4.5 45.8 1.0
N C:ASP288 4.6 26.5 1.0
CG C:ASP291 4.7 36.2 1.0
O10 C:ZOL397 4.7 38.8 1.0
NZ C:LYS301 4.7 17.3 1.0
CE C:LYS301 4.8 20.1 1.0
CA C:ASP288 4.9 26.0 1.0
CA C:ASP287 4.9 23.9 1.0

Magnesium binding site 10 out of 12 in 3ldw

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Magnesium binding site 10 out of 12 in the Crystal Structure of Plasmodium Vivax Geranylgeranylpyrophosphate Synthase PVX_092040 with Zoledronate and Ipp Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 10 of Crystal Structure of Plasmodium Vivax Geranylgeranylpyrophosphate Synthase PVX_092040 with Zoledronate and Ipp Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg1102

b:17.3
occ:1.00
OD2 D:ASP130 2.0 29.4 1.0
O11 D:ZOL397 2.1 17.6 1.0
O D:HOH1200 2.1 13.1 1.0
OD2 D:ASP126 2.1 17.7 1.0
O D:HOH1157 2.2 22.2 1.0
O D:HOH1160 2.4 26.7 1.0
CG D:ASP130 2.7 25.2 1.0
OD1 D:ASP130 2.8 24.1 1.0
MG D:MG1103 3.0 18.1 1.0
CG D:ASP126 3.1 19.9 1.0
OD1 D:ASP126 3.4 17.4 1.0
P9 D:ZOL397 3.4 24.0 1.0
O12 D:ZOL397 3.6 26.4 1.0
OD2 D:ASP198 3.8 35.2 1.0
O D:HOH1158 4.1 30.6 1.0
CB D:ASP130 4.2 22.6 1.0
NE2 D:GLN195 4.3 20.0 1.0
OD1 D:ASP198 4.3 27.6 1.0
CG D:ASP198 4.3 27.7 1.0
O10 D:ZOL397 4.3 24.5 1.0
OE1 D:GLN195 4.4 19.7 1.0
CB D:ASP126 4.4 20.1 1.0
O D:ASP126 4.5 18.2 1.0
O D:HOH1159 4.5 26.3 1.0
NZ D:LYS310 4.6 16.2 1.0
O16 D:ZOL397 4.7 21.1 1.0
C8 D:ZOL397 4.7 10.9 1.0
C19 D:ZOL397 4.7 29.2 1.0
CE D:LYS310 4.7 18.9 1.0
CD D:GLN195 4.8 27.9 1.0
C7 D:ZOL397 4.8 17.4 1.0
N15 D:ZOL397 4.9 24.1 1.0
NZ D:LYS243 4.9 19.2 1.0
CA D:ASP126 4.9 19.0 1.0

Reference:

J.D.Artz, A.K.Wernimont, J.E.Dunford, M.Schapira, A.Dong, Y.Zhao, J.Lew, R.G.Russell, F.H.Ebetino, U.Oppermann, R.Hui. Molecular Characterization of A Novel Geranylgeranyl Pyrophosphate Synthase From Plasmodium Parasites. J.Biol.Chem. V. 286 3315 2011.
ISSN: ISSN 0021-9258
PubMed: 21084289
DOI: 10.1074/JBC.M109.027235
Page generated: Mon Dec 14 08:24:09 2020

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