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Chlorine in PDB 1e2y: Tryparedoxin Peroxidase From Crithidia Fasciculata

Protein crystallography data

The structure of Tryparedoxin Peroxidase From Crithidia Fasciculata, PDB code: 1e2y was solved by M.S.Alphey, C.S.Bond, W.N.Hunter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 21.00 / 3.20
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 123.800, 97.200, 133.800, 90.00, 93.10, 90.00
R / Rfree (%) 27.3 / 28.6

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Tryparedoxin Peroxidase From Crithidia Fasciculata (pdb code 1e2y). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 10 binding sites of Chlorine where determined in the Tryparedoxin Peroxidase From Crithidia Fasciculata, PDB code: 1e2y:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Chlorine binding site 1 out of 10 in 1e2y

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Chlorine binding site 1 out of 10 in the Tryparedoxin Peroxidase From Crithidia Fasciculata


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Tryparedoxin Peroxidase From Crithidia Fasciculata within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1180

b:66.5
occ:1.00
 N B:LEU8 3.8 28.8 1.0
O A:GLY117 4.0 32.6 1.0
CB B:LEU8 4.2 26.8 1.0
CA B:LYS7 4.3 30.0 1.0
CB B:LYS7 4.5 37.1 1.0
C B:LYS7 4.5 26.2 1.0
CD1 A:TYR127 4.6 42.1 1.0
CE1 A:TYR127 4.6 45.3 1.0
CA B:LEU8 4.7 27.3 1.0
CD2 B:LEU8 4.8 23.0 1.0
CD1 B:LEU8 4.8 30.7 1.0
CG B:LEU8 4.9 24.5 1.0
CG B:LYS7 4.9 56.7 1.0
C A:GLY117 5.0 27.9 1.0
O A:LEU119 5.0 33.2 1.0

Chlorine binding site 2 out of 10 in 1e2y

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Chlorine binding site 2 out of 10 in the Tryparedoxin Peroxidase From Crithidia Fasciculata


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Tryparedoxin Peroxidase From Crithidia Fasciculata within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl1180

b:78.7
occ:1.00
 N A:LEU8 3.9 33.5 1.0
O B:GLY117 3.9 33.7 1.0
CB A:LEU8 4.2 19.3 1.0
CA A:LYS7 4.4 47.0 1.0
CB A:LYS7 4.6 57.5 1.0
CE1 B:TYR127 4.6 36.5 1.0
CD1 B:TYR127 4.6 33.7 1.0
C A:LYS7 4.6 43.8 1.0
CA A:LEU8 4.7 28.5 1.0
CD2 A:LEU8 4.8 20.1 1.0
O B:LEU119 4.8 34.4 1.0
C B:GLY117 4.9 30.7 1.0
CG A:LEU8 4.9 19.3 1.0

Chlorine binding site 3 out of 10 in 1e2y

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Chlorine binding site 3 out of 10 in the Tryparedoxin Peroxidase From Crithidia Fasciculata


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Tryparedoxin Peroxidase From Crithidia Fasciculata within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl1180

b:1.0
occ:1.00
 O C:GLY117 3.8 57.8 1.0
N D:LEU8 4.1 66.5 1.0
O D:ALA6 4.4 95.6 1.0
CA D:LYS7 4.5 83.3 1.0
CB D:LEU8 4.6 60.7 1.0
CD1 C:TYR127 4.7 71.7 1.0
CE1 C:TYR127 4.7 79.5 1.0
C C:GLY117 4.8 62.9 1.0
C D:LYS7 4.9 75.8 1.0
CD2 D:LEU8 4.9 75.1 1.0
CB D:LYS7 5.0 92.2 1.0

Chlorine binding site 4 out of 10 in 1e2y

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Chlorine binding site 4 out of 10 in the Tryparedoxin Peroxidase From Crithidia Fasciculata


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Tryparedoxin Peroxidase From Crithidia Fasciculata within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl1180

b:0.1
occ:1.00
 CB C:LYS7 3.7 0.0 1.0
N C:LEU8 3.9 97.1 1.0
O D:GLY117 4.1 64.0 1.0
CA C:LYS7 4.3 0.0 1.0
CB C:LEU8 4.4 84.0 1.0
C C:LYS7 4.6 0.0 1.0
CE1 D:TYR127 4.7 64.9 1.0
CG C:LYS7 4.7 0.0 1.0
CD1 D:TYR127 4.8 65.4 1.0
CA C:LEU8 4.8 90.2 1.0
O D:LEU119 4.8 85.5 1.0
CD2 C:LEU8 5.0 81.5 1.0

Chlorine binding site 5 out of 10 in 1e2y

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Chlorine binding site 5 out of 10 in the Tryparedoxin Peroxidase From Crithidia Fasciculata


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Tryparedoxin Peroxidase From Crithidia Fasciculata within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Cl1180

b:0.7
occ:1.00
 N F:LEU8 3.8 93.9 1.0
O E:GLY117 3.8 72.3 1.0
CA F:LYS7 4.2 0.0 1.0
CB F:LEU8 4.3 79.8 1.0
C F:LYS7 4.5 0.0 1.0
CB F:LYS7 4.6 0.0 1.0
CA F:LEU8 4.7 88.7 1.0
CD1 F:LEU8 4.7 94.0 1.0
CD2 F:LEU8 4.7 85.5 1.0
CD1 F:ILE142 4.7 83.2 1.0
CD1 E:ILE144 4.8 95.6 1.0
CG F:LEU8 4.8 93.0 1.0
CD1 E:TYR127 4.8 86.7 1.0
O F:ALA6 4.8 0.0 1.0
C E:GLY117 4.8 83.3 1.0
CG2 E:ILE144 4.9 91.2 1.0
CE1 E:TYR127 4.9 94.5 1.0

Chlorine binding site 6 out of 10 in 1e2y

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Chlorine binding site 6 out of 10 in the Tryparedoxin Peroxidase From Crithidia Fasciculata


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of Tryparedoxin Peroxidase From Crithidia Fasciculata within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Cl1180

b:0.1
occ:1.00
 N E:LEU8 3.8 0.0 1.0
O F:GLY117 3.9 54.2 1.0
CA E:LYS7 4.2 0.0 1.0
CB E:LEU8 4.3 0.0 1.0
CB E:LYS7 4.4 0.0 1.0
C E:LYS7 4.5 0.0 1.0
CA E:LEU8 4.7 0.0 1.0
CD1 F:TYR127 4.8 97.2 1.0
CE1 F:TYR127 4.8 98.0 1.0
CG E:LYS7 4.8 0.0 1.0
O F:LEU119 4.8 0.0 1.0
C F:GLY117 4.9 56.0 1.0
CD1 E:LEU8 4.9 0.0 1.0
O E:ALA6 4.9 0.0 1.0
CD2 E:LEU8 4.9 0.0 1.0
CG E:LEU8 5.0 0.0 1.0

Chlorine binding site 7 out of 10 in 1e2y

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Chlorine binding site 7 out of 10 in the Tryparedoxin Peroxidase From Crithidia Fasciculata


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 7 of Tryparedoxin Peroxidase From Crithidia Fasciculata within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Cl1180

b:87.9
occ:1.00
 N H:LEU8 3.8 66.7 1.0
O G:GLY117 3.9 65.6 1.0
CB H:LEU8 4.2 51.5 1.0
CA H:LYS7 4.3 67.7 1.0
CB H:LYS7 4.4 73.7 1.0
C H:LYS7 4.6 68.2 1.0
CA H:LEU8 4.6 59.0 1.0
CE1 G:TYR127 4.7 55.8 1.0
CD1 G:TYR127 4.7 51.3 1.0
O G:LEU119 4.7 56.1 1.0
CD2 H:LEU8 4.8 49.6 1.0
C G:GLY117 4.9 59.3 1.0
CG H:LYS7 4.9 90.0 1.0
CG H:LEU8 4.9 52.6 1.0
CD1 H:LEU8 5.0 58.5 1.0

Chlorine binding site 8 out of 10 in 1e2y

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Chlorine binding site 8 out of 10 in the Tryparedoxin Peroxidase From Crithidia Fasciculata


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 8 of Tryparedoxin Peroxidase From Crithidia Fasciculata within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Cl1180

b:74.7
occ:1.00
 N G:LEU8 3.8 48.1 1.0
O H:GLY117 3.9 44.9 1.0
CA G:LYS7 4.3 59.6 1.0
CB G:LEU8 4.3 43.4 1.0
CB G:LYS7 4.5 72.9 1.0
C G:LYS7 4.6 56.8 1.0
CD1 H:TYR127 4.6 50.7 1.0
CE1 H:TYR127 4.7 60.9 1.0
CA G:LEU8 4.7 46.3 1.0
CD2 G:LEU8 4.9 48.6 1.0
C H:GLY117 4.9 36.8 1.0
CG G:LYS7 4.9 84.2 1.0
CD1 G:LEU8 4.9 36.5 1.0
O H:LEU119 5.0 33.4 1.0
CG G:LEU8 5.0 40.5 1.0

Chlorine binding site 9 out of 10 in 1e2y

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Chlorine binding site 9 out of 10 in the Tryparedoxin Peroxidase From Crithidia Fasciculata


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 9 of Tryparedoxin Peroxidase From Crithidia Fasciculata within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Cl1180

b:54.1
occ:1.00
 N J:LEU8 3.8 25.8 1.0
O I:GLY117 3.9 40.0 1.0
CA J:LYS7 4.2 36.0 1.0
CB J:LEU8 4.3 16.9 1.0
CB J:LYS7 4.4 45.1 1.0
C J:LYS7 4.5 28.6 1.0
CE1 I:TYR127 4.7 40.8 1.0
CA J:LEU8 4.7 24.0 1.0
CD1 I:TYR127 4.7 30.9 1.0
CG J:LYS7 4.8 60.8 1.0
C I:GLY117 4.8 39.0 1.0
O I:LEU119 4.9 35.5 1.0
CD2 J:LEU8 4.9 34.4 1.0
CD1 J:LEU8 5.0 33.3 1.0

Chlorine binding site 10 out of 10 in 1e2y

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Chlorine binding site 10 out of 10 in the Tryparedoxin Peroxidase From Crithidia Fasciculata


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 10 of Tryparedoxin Peroxidase From Crithidia Fasciculata within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Cl1180

b:60.2
occ:1.00
 N I:LEU8 3.7 29.4 1.0
O J:GLY117 4.1 29.9 1.0
CB I:LEU8 4.1 15.4 1.0
CA I:LYS7 4.2 36.1 1.0
C I:LYS7 4.5 27.7 1.0
CB I:LYS7 4.5 42.0 1.0
CA I:LEU8 4.6 23.6 1.0
CD1 J:TYR127 4.6 37.1 1.0
CE1 J:TYR127 4.6 44.5 1.0
CD2 I:LEU8 4.8 25.7 1.0
CG I:LEU8 4.8 20.8 1.0
CD1 I:LEU8 4.8 22.3 1.0
CG I:LYS7 4.9 56.0 1.0

Reference:

M.S.Alphey, C.S.Bond, E.Tetaud, A.H.Fairlamb, W.N.Hunter. The Structure of Reduced Tryparedoxin Peroxidase Reveals A Decamer and Insight Into Reactivity of 2CYS-Peroxiredoxins J.Mol.Biol. V. 300 903 2000.
ISSN: ISSN 0022-2836
PubMed: 10891277
DOI: 10.1006/JMBI.2000.3881
Page generated: Fri Jul 19 21:43:19 2024

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