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Bromine in PDB 9hsy: Crystal Structure of C-Terminal Catalytic Domain of Plasmodium Falciparum Ctp:Phosphocholine Cytidylyltransferase with 4- Bromopyrazole

Enzymatic activity of Crystal Structure of C-Terminal Catalytic Domain of Plasmodium Falciparum Ctp:Phosphocholine Cytidylyltransferase with 4- Bromopyrazole

All present enzymatic activity of Crystal Structure of C-Terminal Catalytic Domain of Plasmodium Falciparum Ctp:Phosphocholine Cytidylyltransferase with 4- Bromopyrazole:
2.7.7.15;

Protein crystallography data

The structure of Crystal Structure of C-Terminal Catalytic Domain of Plasmodium Falciparum Ctp:Phosphocholine Cytidylyltransferase with 4- Bromopyrazole, PDB code: 9hsy was solved by S.Audebert, M.Gelin, J.-F.Guichou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.83 / 2.10
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 50.432, 70.809, 119.252, 90, 90, 90
R / Rfree (%) 21.2 / 24.8

Bromine Binding Sites:

The binding sites of Bromine atom in the Crystal Structure of C-Terminal Catalytic Domain of Plasmodium Falciparum Ctp:Phosphocholine Cytidylyltransferase with 4- Bromopyrazole (pdb code 9hsy). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Crystal Structure of C-Terminal Catalytic Domain of Plasmodium Falciparum Ctp:Phosphocholine Cytidylyltransferase with 4- Bromopyrazole, PDB code: 9hsy:

Bromine binding site 1 out of 1 in 9hsy

Go back to Bromine Binding Sites List in 9hsy
Bromine binding site 1 out of 1 in the Crystal Structure of C-Terminal Catalytic Domain of Plasmodium Falciparum Ctp:Phosphocholine Cytidylyltransferase with 4- Bromopyrazole


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of C-Terminal Catalytic Domain of Plasmodium Falciparum Ctp:Phosphocholine Cytidylyltransferase with 4- Bromopyrazole within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br801

b:118.3
occ:1.00
 BR4 A:BYZ801 0.0 118.3 1.0
C4 A:BYZ801 1.9 81.5 1.0
C5 A:BYZ801 2.9 83.4 1.0
C3 A:BYZ801 3.0 79.9 1.0
H3 A:BYZ801 3.3 96.1 1.0
H1 A:BYZ801 3.3 100.4 1.0
C A:GLY632 3.7 45.2 1.0
CG A:ARG755 3.8 88.4 1.0
CE1 A:HIS630 3.8 51.8 1.0
CA A:GLY632 3.9 45.0 1.0
O A:GLY632 3.9 43.6 1.0
CB A:ARG755 4.0 88.2 1.0
N1 A:BYZ801 4.1 86.2 1.0
N2 A:BYZ801 4.1 80.2 1.0
N A:HIS633 4.1 43.9 1.0
O A:THR756 4.1 78.5 1.0
OE1 A:GLN636 4.2 57.9 1.0
N A:THR756 4.2 73.5 1.0
CA A:ARG755 4.3 87.1 1.0
O A:HOH921 4.5 48.2 1.0
NE2 A:HIS630 4.6 52.6 1.0
NE A:ARG755 4.6 91.1 1.0
CZ A:ARG755 4.7 94.0 1.0
CD A:ARG755 4.8 88.9 1.0
CA A:HIS633 4.8 40.4 1.0
ND1 A:HIS630 4.8 51.1 1.0
C A:ARG755 4.8 90.7 1.0
NH1 A:ARG755 4.9 93.5 1.0
C A:THR756 5.0 76.9 1.0

Reference:

S.Audebert, M.Gelin, J.-F.Guichou. Crystal Structure of C-Terminal Catalytic Domain of Plasmodium Falciparum Ctp:Phosphocholine Cytidylyltransferase with 4-Bromopyrazole To Be Published.
Page generated: Mon Jul 7 13:01:17 2025

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