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Chlorine in PDB 4twa: Crystal Structure of Prolyl-Trna Synthetase (Prs) From Plasmodium Falciparum

Enzymatic activity of Crystal Structure of Prolyl-Trna Synthetase (Prs) From Plasmodium Falciparum

All present enzymatic activity of Crystal Structure of Prolyl-Trna Synthetase (Prs) From Plasmodium Falciparum:
6.1.1.15;

Protein crystallography data

The structure of Crystal Structure of Prolyl-Trna Synthetase (Prs) From Plasmodium Falciparum, PDB code: 4twa was solved by V.Jain, M.Yogavel, A.Sharma, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.79 / 3.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 133.240, 104.106, 111.420, 90.00, 92.30, 90.00
R / Rfree (%) 17.2 / 24.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Prolyl-Trna Synthetase (Prs) From Plasmodium Falciparum (pdb code 4twa). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 6 binding sites of Chlorine where determined in the Crystal Structure of Prolyl-Trna Synthetase (Prs) From Plasmodium Falciparum, PDB code: 4twa:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6;

Chlorine binding site 1 out of 6 in 4twa

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Chlorine binding site 1 out of 6 in the Crystal Structure of Prolyl-Trna Synthetase (Prs) From Plasmodium Falciparum


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 (Prs) From Plasmodium Falciparum within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl801

b:44.4
occ:1.00
 CL A:CL802 3.2 53.1 1.0
NH2 A:ARG403 3.2 71.9 1.0
N A:LYS394 3.8 60.4 1.0
NH1 A:ARG403 3.9 69.7 1.0
CZ A:ARG403 3.9 68.5 1.0
CD1 A:PHE393 4.0 60.9 1.0
NZ A:LYS327 4.1 76.3 1.0
CB A:LYS394 4.3 71.5 1.0
CA A:PHE393 4.3 40.4 1.0
CG A:LYS394 4.4 73.8 1.0
C A:PHE393 4.6 46.6 1.0
CD A:LYS394 4.6 71.1 1.0
CA A:LYS394 4.7 59.8 1.0
CE1 A:PHE393 4.7 61.2 1.0
CE A:LYS327 4.8 73.2 1.0
CB A:PHE393 4.9 41.5 1.0
CG A:PHE393 4.9 50.6 1.0

Chlorine binding site 2 out of 6 in 4twa

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Chlorine binding site 2 out of 6 in the Crystal Structure of Prolyl-Trna Synthetase (Prs) From Plasmodium Falciparum


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 (Prs) From Plasmodium Falciparum within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl802

b:53.1
occ:1.00
 CL A:CL801 3.2 44.4 1.0
NH2 A:ARG401 3.4 64.2 1.0
N A:LYS394 3.5 60.4 1.0
CB A:LYS394 3.7 71.5 1.0
NH1 A:ARG401 3.8 64.4 1.0
N A:GLN395 3.9 58.4 1.0
CG A:GLN395 4.0 95.0 1.0
CD1 A:PHE393 4.0 60.9 1.0
CZ A:ARG401 4.1 62.6 1.0
CA A:LYS394 4.1 59.8 1.0
CB A:PHE393 4.2 41.5 1.0
CG A:PHE393 4.5 50.6 1.0
C A:PHE393 4.5 46.6 1.0
CA A:PHE393 4.6 40.4 1.0
C A:LYS394 4.6 53.5 1.0
NE2 A:GLN395 4.7 0.8 1.0
CG A:LYS394 4.7 73.8 1.0
CE1 A:PHE393 4.9 61.2 1.0
CD A:LYS394 4.9 71.1 1.0
CA A:GLN395 4.9 68.0 1.0
CD A:GLN395 4.9 0.7 1.0
O A:GLN395 5.0 49.4 1.0

Chlorine binding site 3 out of 6 in 4twa

Go back to Chlorine Binding Sites List in 4twa
Chlorine binding site 3 out of 6 in the Crystal Structure of Prolyl-Trna Synthetase (Prs) From Plasmodium Falciparum


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Prolyl-Trna Synthetase (Prs) From Plasmodium Falciparum within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl803

b:44.0
occ:0.71
 NZ A:LYS381 3.1 36.9 1.0
ND2 A:ASN310 3.6 61.8 1.0
CG A:PRO379 3.9 46.1 1.0
CE A:LYS381 4.3 32.9 1.0
CD A:PRO379 4.4 47.3 1.0
CB A:ASN310 4.5 45.5 1.0
CG A:ASN310 4.5 57.6 1.0
CD A:LYS381 5.0 30.1 1.0

Chlorine binding site 4 out of 6 in 4twa

Go back to Chlorine Binding Sites List in 4twa
Chlorine binding site 4 out of 6 in the Crystal Structure of Prolyl-Trna Synthetase (Prs) From Plasmodium Falciparum


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of Prolyl-Trna Synthetase (Prs) From Plasmodium Falciparum within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl801

b:58.8
occ:0.65
 CL B:CL802 3.3 66.5 1.0
N B:LYS394 3.9 62.5 1.0
CD1 B:PHE393 4.0 53.0 1.0
CB B:LYS394 4.0 66.6 1.0
NH2 B:ARG403 4.2 82.5 1.0
NH2 B:ARG401 4.6 75.6 1.0
CE1 B:PHE393 4.6 49.2 1.0
CA B:LYS394 4.6 68.8 1.0
CA B:PHE393 4.8 64.1 1.0
C B:PHE393 4.9 63.9 1.0
CZ B:ARG403 4.9 76.1 1.0
NH1 B:ARG403 4.9 72.5 1.0
CG B:PHE393 4.9 55.6 1.0

Chlorine binding site 5 out of 6 in 4twa

Go back to Chlorine Binding Sites List in 4twa
Chlorine binding site 5 out of 6 in the Crystal Structure of Prolyl-Trna Synthetase (Prs) From Plasmodium Falciparum


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Crystal Structure of Prolyl-Trna Synthetase (Prs) From Plasmodium Falciparum within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl802

b:66.5
occ:1.00
 N B:GLN395 2.9 84.3 1.0
NH1 B:ARG401 3.0 76.6 1.0
CB B:LYS394 3.3 66.6 1.0
N B:LYS394 3.3 62.5 1.0
CL B:CL801 3.3 58.8 0.7
NH2 B:ARG401 3.4 75.6 1.0
CA B:LYS394 3.6 68.8 1.0
CZ B:ARG401 3.6 75.4 1.0
C B:LYS394 3.7 73.2 1.0
CA B:GLN395 3.8 84.7 1.0
CB B:GLN395 3.9 84.3 1.0
CB B:PHE393 4.0 55.8 1.0
O B:GLN395 4.1 82.3 1.0
C B:PHE393 4.2 63.9 1.0
C B:GLN395 4.2 80.4 1.0
CD1 B:PHE393 4.4 53.0 1.0
CG B:PHE393 4.4 55.6 1.0
CA B:PHE393 4.5 64.1 1.0
O B:LYS394 4.9 61.1 1.0
NE B:ARG401 5.0 70.1 1.0

Chlorine binding site 6 out of 6 in 4twa

Go back to Chlorine Binding Sites List in 4twa
Chlorine binding site 6 out of 6 in the Crystal Structure of Prolyl-Trna Synthetase (Prs) From Plasmodium Falciparum


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of Crystal Structure of Prolyl-Trna Synthetase (Prs) From Plasmodium Falciparum within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl803

b:45.4
occ:0.92
 ND2 B:ASN310 3.2 66.6 1.0
NZ B:LYS381 3.3 37.2 1.0
CG B:PRO379 3.9 38.0 1.0
CB B:ASN310 4.1 42.6 1.0
CG B:ASN310 4.1 57.0 1.0
CE B:LYS381 4.2 39.3 1.0
CD B:PRO379 4.4 38.5 1.0
CD B:LYS381 5.0 27.5 1.0

Reference:

V.Jain, H.Kikuchi, Y.Oshima, A.Sharma, M.Yogavel. Structural and Functional Analysis of the Anti-Malarial Drug Target Prolyl-Trna Synthetase. J. Struct. Funct. Genomics 2014.
ISSN: ISSN 1570-0267
PubMed: 25047712
DOI: 10.1007/S10969-014-9186-X
Page generated: Sat Dec 12 11:14:02 2020

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