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Manganese in PDB 9hsh: Crystal Structure of C-Terminal Catalytic Domain of Plasmodium Falciparum Ctp:Phosphocholine Cytidylyltransferase with Cytidine- Triphosphate

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

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

Protein crystallography data

The structure of Crystal Structure of C-Terminal Catalytic Domain of Plasmodium Falciparum Ctp:Phosphocholine Cytidylyltransferase with Cytidine- Triphosphate, PDB code: 9hsh 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) 59.64 / 1.80
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 50.494, 69.321, 117.043, 90, 90, 90
R / Rfree (%) 23.1 / 25.7

Manganese Binding Sites:

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

Manganese binding site 1 out of 1 in 9hsh

Go back to Manganese Binding Sites List in 9hsh
Manganese binding site 1 out of 1 in the Crystal Structure of C-Terminal Catalytic Domain of Plasmodium Falciparum Ctp:Phosphocholine Cytidylyltransferase with Cytidine- Triphosphate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of C-Terminal Catalytic Domain of Plasmodium Falciparum Ctp:Phosphocholine Cytidylyltransferase with Cytidine- Triphosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn802

b:30.0
occ:1.00
O1A A:CTP801 2.5 50.8 0.5
O1G A:CTP801 2.5 55.5 0.5
O1A A:CTP801 2.8 51.5 0.5
N A:ASP627 3.1 43.6 1.0
O1B A:CTP801 3.5 55.9 0.5
NE2 A:HIS633 3.5 39.7 1.0
N A:TYR626 3.5 45.3 1.0
O A:HOH910 3.6 52.1 1.0
CB A:ASP627 3.6 46.5 1.0
PA A:CTP801 3.7 50.8 0.5
O2B A:CTP801 3.7 56.4 0.5
CB A:VAL625 3.8 44.6 1.0
PG A:CTP801 3.8 51.8 0.5
O3A A:CTP801 3.8 54.7 0.5
CA A:ASP627 3.8 45.7 1.0
PA A:CTP801 3.8 50.8 0.5
O1G A:CTP801 3.8 68.8 0.5
O A:ASP627 3.9 47.2 1.0
CE1 A:HIS633 3.9 42.7 1.0
CA A:TYR626 3.9 47.1 1.0
C A:TYR626 4.0 50.5 1.0
CG1 A:VAL625 4.0 47.3 1.0
O3B A:CTP801 4.1 54.6 0.5
PB A:CTP801 4.2 55.5 0.5
O3A A:CTP801 4.2 54.8 0.5
O3G A:CTP801 4.2 62.0 0.5
O3B A:CTP801 4.2 54.0 0.5
PB A:CTP801 4.2 57.1 0.5
C A:VAL625 4.2 45.0 1.0
O2G A:CTP801 4.3 67.3 0.5
C A:ASP627 4.3 48.1 1.0
PG A:CTP801 4.3 54.0 0.5
CA A:VAL625 4.5 42.9 1.0
O2A A:CTP801 4.6 50.7 0.5
CD2 A:HIS633 4.7 37.8 1.0
CG2 A:VAL625 4.8 44.8 1.0
O5' A:CTP801 4.9 53.7 0.5
O5' A:CTP801 4.9 56.7 0.5
N A:VAL625 4.9 40.8 1.0

Reference:

S.Audebert, M.Gelin, J.-F.Guichou. Crystal Structure of C-Terminal Catalytic Domain of Plasmodium Falciparum Ctp:Phosphocholine Cytidylyltransferase with Cytidine-Triphosphate To Be Published.
Page generated: Sun Feb 9 08:28:35 2025

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