Atomistry » Zinc » PDB 3lt8-3m1j » 3lze
Atomistry »
  Zinc »
    PDB 3lt8-3m1j »
      3lze »

Zinc in PDB 3lze: Plasmodium Vivax 6-Pyruvoyltetrahydropterin Synthase (Ptps), E37C Catalytic Residue Mutant

Enzymatic activity of Plasmodium Vivax 6-Pyruvoyltetrahydropterin Synthase (Ptps), E37C Catalytic Residue Mutant

All present enzymatic activity of Plasmodium Vivax 6-Pyruvoyltetrahydropterin Synthase (Ptps), E37C Catalytic Residue Mutant:
4.2.3.12;

Protein crystallography data

The structure of Plasmodium Vivax 6-Pyruvoyltetrahydropterin Synthase (Ptps), E37C Catalytic Residue Mutant, PDB code: 3lze was solved by E.T.Larson, E.A.Merritt, Medical Structural Genomics Of Pathogenicprotozoa (Msgpp), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.03 / 1.90
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 131.495, 131.495, 73.670, 90.00, 90.00, 120.00
R / Rfree (%) 19.1 / 22

Zinc Binding Sites:

The binding sites of Zinc atom in the Plasmodium Vivax 6-Pyruvoyltetrahydropterin Synthase (Ptps), E37C Catalytic Residue Mutant (pdb code 3lze). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Plasmodium Vivax 6-Pyruvoyltetrahydropterin Synthase (Ptps), E37C Catalytic Residue Mutant, PDB code: 3lze:

Zinc binding site 1 out of 1 in 3lze

Go back to Zinc Binding Sites List in 3lze
Zinc binding site 1 out of 1 in the Plasmodium Vivax 6-Pyruvoyltetrahydropterin Synthase (Ptps), E37C Catalytic Residue Mutant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Plasmodium Vivax 6-Pyruvoyltetrahydropterin Synthase (Ptps), E37C Catalytic Residue Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn201

b:47.8
occ:1.00
 NE2 A:HIS40 2.0 43.5 1.0
NE2 A:HIS42 2.1 41.6 1.0
NE2 A:HIS28 2.1 39.1 1.0
O A:HOH231 2.2 54.5 1.0
OE2 A:GLU160 2.9 56.0 0.5
CE1 A:HIS28 2.9 37.8 1.0
CD2 A:HIS40 3.0 44.0 1.0
CE1 A:HIS40 3.0 49.4 1.0
CD2 A:HIS42 3.0 43.3 1.0
CE1 A:HIS42 3.1 44.0 1.0
CD2 A:HIS28 3.2 39.6 1.0
CD A:GLU160 3.8 61.0 0.5
ND1 A:HIS40 4.1 44.4 1.0
CG A:HIS40 4.1 39.8 1.0
ND1 A:HIS28 4.1 37.4 1.0
CG A:HIS42 4.2 43.5 1.0
OE2 A:GLU160 4.2 51.0 0.5
ND1 A:HIS42 4.2 44.5 1.0
CG A:HIS28 4.3 37.0 1.0
OE1 A:GLU160 4.4 59.8 0.5
C5 A:PE0211 4.5 67.7 1.0
CG A:GLU160 4.6 58.0 0.5
N4 A:PE0211 4.7 61.8 1.0
CD A:GLU160 4.7 52.0 0.5
O A:HOH225 4.7 46.4 1.0
OE1 A:GLU160 4.7 55.8 0.5
OH A:TYR44 4.8 45.7 1.0
CG1 A:ILE30 5.0 53.0 0.6

Reference:

E.T.Larson, J.Bosch, J.E.Kim, A.Kelley, L.Castaneda, A.Napuli, N.Mueller, C.L.M.J.Verlinde, W.C.Van Voorhis, F.S.Buckner, E.Fan, W.G.J.Hol, E.A.Merritt. Structural Analysis of the Dual-Functional 6-Pyruvoyltetrahydropterin Synthase From Malaria Parasites. To Be Published.
Page generated: Sat Oct 26 08:58:14 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