Chlorine in PDB 5ifu: Crystal Structure of Prolyl-Trna Synthetase (Prors, Proline--Trna Ligase) From Plasmodium Falciparum in Complex with Glyburide

All present enzymatic activity of Crystal Structure of Prolyl-Trna Synthetase (Prors, Proline--Trna Ligase) From Plasmodium Falciparum in Complex with Glyburide:
6.1.1.15;

The structure of Crystal Structure of Prolyl-Trna Synthetase (Prors, Proline--Trna Ligase) From Plasmodium Falciparum in Complex with Glyburide, PDB code: 5ifu was solved by D.M.Dranow, S.N.Hewitt, J.Abendroth, Structural Genomics Consortium(Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.74 / 2.45
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	138.310, 138.310, 156.660, 90.00, 90.00, 90.00
R / Rfree (%)	18.5 / 21.3

The binding sites of Chlorine atom in the Crystal Structure of Prolyl-Trna Synthetase (Prors, Proline--Trna Ligase) From Plasmodium Falciparum in Complex with Glyburide (pdb code 5ifu). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Prolyl-Trna Synthetase (Prors, Proline--Trna Ligase) From Plasmodium Falciparum in Complex with Glyburide, PDB code: 5ifu:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Prolyl-Trna Synthetase (Prors, Proline--Trna Ligase) From Plasmodium Falciparum in Complex with Glyburide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Prolyl-Trna Synthetase (Prors, Proline--Trna Ligase) From Plasmodium Falciparum in Complex with Glyburide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl801 b:0.8 occ:1.00 CL1 A:GBM801 0.0 0.8 1.0 C31 A:GBM801 1.8 1.0 1.0 C29 A:GBM801 2.7 0.8 1.0 C32 A:GBM801 2.8 0.8 1.0 CB A:PHE262 3.9 54.4 1.0 C27 A:GBM801 4.0 0.9 1.0 C30 A:GBM801 4.1 0.6 1.0 CB A:ASN470 4.2 61.3 1.0 C28 A:GBM801 4.6 0.9 1.0 ND2 A:ASN470 4.6 72.4 1.0 CG A:PHE262 4.7 53.6 1.0 N A:SER263 4.7 59.6 1.0 N A:PHE262 4.7 62.2 1.0 CA A:PHE262 4.8 57.4 1.0 CD2 A:PHE262 4.8 54.4 1.0 CG A:ASN470 5.0 69.5 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Prolyl-Trna Synthetase (Prors, Proline--Trna Ligase) From Plasmodium Falciparum in Complex with Glyburide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Prolyl-Trna Synthetase (Prors, Proline--Trna Ligase) From Plasmodium Falciparum in Complex with Glyburide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl802 b:39.5 occ:1.00 OG A:SER366 3.1 35.0 1.0 O A:HOH982 3.2 39.7 1.0 N A:SER366 3.3 33.5 1.0 N A:MET364 3.3 32.3 1.0 CB A:SER366 3.5 32.5 1.0 N A:TYR365 3.6 31.7 1.0 CG2 A:ILE363 3.9 33.6 1.0 CA A:ILE363 3.9 35.0 1.0 CA A:SER366 4.0 36.0 1.0 C A:ILE363 4.1 34.5 1.0 C A:MET364 4.1 34.9 1.0 CZ A:PHE490 4.2 36.5 1.0 C A:TYR365 4.2 38.1 1.0 CA A:TYR365 4.2 33.5 1.0 CA A:MET364 4.3 33.8 1.0 CB A:TYR365 4.4 33.2 1.0 CB A:ILE363 4.4 34.6 1.0 CE2 A:PHE490 4.6 43.0 1.0 O A:THR362 4.7 36.5 1.0 CE1 A:PHE490 4.7 45.2 1.0 CG1 A:ILE363 4.8 39.8 1.0 O A:MET364 4.9 36.3 1.0

S.N.Hewitt, D.M.Dranow, B.G.Horst, J.A.Abendroth, B.Forte, I.Hallyburton, C.Jansen, B.Baragana, R.Choi, K.L.Rivas, M.A.Hulverson, M.Dumais, T.E.Edwards, D.D.Lorimer, A.H.Fairlamb, D.W.Gray, K.D.Read, A.M.Lehane, K.Kirk, P.J.Myler, A.Wernimont, C.Walpole, R.Stacy, L.K.Barrett, I.H.Gilbert, W.C.Van Voorhis. Biochemical and Structural Characterization of Selective Allosteric Inhibitors of the Plasmodium Falciparum Drug Target, Prolyl-Trna-Synthetase. Acs Infect Dis V. 3 34 2017.
ISSN: ESSN 2373-8227
PubMed: 27798837
DOI: 10.1021/ACSINFECDIS.6B00078