Potassium in PDB 4jfa: Crystal Structure of Plasmodium Falciparum Tryptophanyl-Trna Synthetase

All present enzymatic activity of Crystal Structure of Plasmodium Falciparum Tryptophanyl-Trna Synthetase:
6.1.1.2;

The structure of Crystal Structure of Plasmodium Falciparum Tryptophanyl-Trna Synthetase, PDB code: 4jfa was solved by S.Khan, A.Garg, Y.Manickam, A.Sharma, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.83 / 2.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	51.176, 213.252, 101.952, 90.00, 97.15, 90.00
R / Rfree (%)	19.1 / 22.9

The binding sites of Potassium atom in the Crystal Structure of Plasmodium Falciparum Tryptophanyl-Trna Synthetase (pdb code 4jfa). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of Plasmodium Falciparum Tryptophanyl-Trna Synthetase, PDB code: 4jfa:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Crystal Structure of Plasmodium Falciparum Tryptophanyl-Trna Synthetase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of Plasmodium Falciparum Tryptophanyl-Trna Synthetase within 5.0Å range: probe atom residue distance (Å) B Occ C:K702 b:61.4 occ:1.00 O C:HOH801 2.9 29.8 1.0 O A:HOH803 3.0 36.5 1.0 O A:HOH804 3.4 34.5 1.0 O B:HOH836 3.6 33.2 1.0 OH C:TYR348 3.7 26.2 1.0 NZ A:LYS402 4.2 28.3 1.0 ND2 B:ASN295 4.2 44.1 1.0 O B:HOH805 4.5 54.0 1.0 CE1 C:TYR348 4.5 33.1 1.0 CZ C:TYR348 4.6 30.9 1.0 CB C:SER355 4.7 28.5 1.0 O A:HOH858 4.7 42.9 1.0 CA C:SER355 4.8 34.8 1.0

Potassium binding site 2 out of 2 in the Crystal Structure of Plasmodium Falciparum Tryptophanyl-Trna Synthetase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of Plasmodium Falciparum Tryptophanyl-Trna Synthetase within 5.0Å range: probe atom residue distance (Å) B Occ D:K703 b:63.6 occ:1.00 O B:HOH863 2.9 48.9 1.0 O B:HOH864 3.0 55.7 1.0 O D:HOH810 3.1 35.8 1.0 OH D:TYR348 3.5 26.8 1.0 NZ B:LYS402 3.9 25.2 1.0 CE1 D:TYR348 4.3 35.9 1.0 CZ D:TYR348 4.4 34.0 1.0 O B:HOH801 4.7 28.2 1.0 OG B:SER398 4.7 36.4 1.0 CB D:SER355 4.8 40.8 1.0 CA D:SER355 4.8 32.3 1.0 CE B:LYS402 4.9 31.9 1.0

S.Khan, A.Garg, A.Sharma, N.Camacho, D.Picchioni, A.Saint-Leger, L.Ribas De Pouplana, M.Yogavel, A.Sharma. An Appended Domain Results in An Unusual Architecture For Malaria Parasite Tryptophanyl-Trna Synthetase Plos One V. 8 66224 2013.
ISSN: ESSN 1932-6203
PubMed: 23776638
DOI: 10.1371/JOURNAL.PONE.0066224