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Chlorine in PDB 1nsl: Crystal Structure of Probable Acetyltransferase

Protein crystallography data

The structure of Crystal Structure of Probable Acetyltransferase, PDB code: 1nsl was solved by J.S.Brunzelle, S.V.Korolev, R.Wu, A.Joachimiak, W.F.Anderson, Midwestcenter For Structural Genomics (Mcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 59.339, 134.185, 91.062, 90.00, 104.08, 90.00
R / Rfree (%) 25.6 / 27.8

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Probable Acetyltransferase (pdb code 1nsl). 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 Probable Acetyltransferase, PDB code: 1nsl:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6;

Chlorine binding site 1 out of 6 in 1nsl

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Chlorine binding site 1 out of 6 in the Crystal Structure of Probable Acetyltransferase


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 Probable Acetyltransferase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl184

b:82.4
occ:1.00
OG1 A:THR111 3.5 27.9 1.0
N A:THR111 3.7 28.1 1.0
CA A:GLY108 3.7 32.2 1.0
N A:ILE110 3.7 31.3 1.0
C A:GLY108 3.8 33.0 1.0
N A:ILE109 3.8 32.7 1.0
CB A:ILE110 3.8 28.4 1.0
CA A:ILE110 4.2 29.3 1.0
N A:GLY108 4.3 32.1 1.0
CB A:THR111 4.3 27.5 1.0
CG1 A:ILE110 4.4 26.9 1.0
C A:ILE109 4.4 32.6 1.0
NH2 A:ARG147 4.4 38.8 1.0
O A:GLY108 4.4 33.2 1.0
C A:ILE110 4.4 29.3 1.0
CG2 A:VAL144 4.6 26.4 1.0
CA A:THR111 4.6 27.7 1.0
CA A:ILE109 4.6 32.8 1.0
CD1 A:ILE110 4.9 18.2 1.0
CG2 A:ILE110 5.0 30.6 1.0

Chlorine binding site 2 out of 6 in 1nsl

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Chlorine binding site 2 out of 6 in the Crystal Structure of Probable Acetyltransferase


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 Probable Acetyltransferase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl184

b:80.4
occ:1.00
CA B:GLY108 3.2 33.0 1.0
N B:ILE109 3.3 32.2 1.0
C B:GLY108 3.4 32.5 1.0
N B:ILE110 3.4 31.6 1.0
N B:GLY108 3.6 33.5 1.0
CB B:ILE110 3.9 31.1 1.0
N B:THR111 4.0 29.9 1.0
C B:ILE109 4.1 32.1 1.0
CA B:ILE110 4.1 31.2 1.0
CA B:ILE109 4.2 32.3 1.0
O B:GLY108 4.2 32.2 1.0
CG1 B:ILE110 4.2 30.0 1.0
OG1 B:THR111 4.3 27.1 1.0
O B:GLU105 4.4 28.8 1.0
C B:ILE110 4.6 31.0 1.0
CD1 B:ILE110 4.6 30.6 1.0
C B:LYS107 4.7 33.4 1.0
CB B:ILE109 4.8 31.9 1.0
CB B:THR111 4.8 29.3 1.0

Chlorine binding site 3 out of 6 in 1nsl

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Chlorine binding site 3 out of 6 in the Crystal Structure of Probable Acetyltransferase


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 Probable Acetyltransferase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl184

b:74.4
occ:1.00
CA C:GLY108 3.3 30.7 1.0
OG1 C:THR111 3.4 32.4 1.0
N C:THR111 3.5 31.1 1.0
C C:GLY108 3.7 31.9 1.0
N C:ILE110 3.8 32.0 1.0
N C:GLY108 3.9 29.9 1.0
CB C:THR111 4.0 31.2 1.0
N C:ILE109 4.0 31.7 1.0
CB C:ILE110 4.1 30.4 1.0
CG2 C:VAL144 4.2 33.2 1.0
CA C:ILE110 4.2 31.1 1.0
CA C:THR111 4.4 30.8 1.0
O C:GLY108 4.4 32.3 1.0
C C:ILE110 4.4 31.6 1.0
C C:ILE109 4.6 32.7 1.0
CG1 C:ILE110 4.8 32.1 1.0
CA C:ILE109 5.0 32.4 1.0

Chlorine binding site 4 out of 6 in 1nsl

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Chlorine binding site 4 out of 6 in the Crystal Structure of Probable Acetyltransferase


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 Probable Acetyltransferase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl184

b:81.5
occ:0.75
CB D:ILE110 4.1 26.6 1.0
N D:ILE110 4.1 27.9 1.0
N D:THR111 4.2 29.2 1.0
CA D:GLY108 4.2 30.1 1.0
OG1 D:THR111 4.4 32.5 1.0
N D:ILE109 4.4 28.9 1.0
CG2 D:VAL144 4.4 24.7 1.0
N D:GLY108 4.5 30.1 1.0
C D:GLY108 4.5 29.4 1.0
CA D:ILE110 4.5 27.4 1.0
CG1 D:ILE110 4.7 22.9 1.0
CB D:THR111 4.8 30.6 1.0
CD1 D:ILE110 4.8 14.7 1.0
C D:ILE110 4.9 28.3 1.0

Chlorine binding site 5 out of 6 in 1nsl

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Chlorine binding site 5 out of 6 in the Crystal Structure of Probable Acetyltransferase


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 Probable Acetyltransferase within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Cl184

b:84.6
occ:0.60
N E:ILE110 3.2 28.6 1.0
OG1 E:THR111 3.3 29.7 1.0
CB E:ILE110 3.5 28.8 1.0
CA E:GLY108 3.6 30.8 1.0
C E:GLY108 3.6 30.2 1.0
N E:ILE109 3.7 29.3 1.0
N E:THR111 3.7 29.3 1.0
CG1 E:ILE110 3.8 27.7 1.0
CA E:ILE110 3.8 29.4 1.0
N E:GLY108 4.1 31.4 1.0
C E:ILE109 4.1 28.8 1.0
O E:GLY108 4.2 30.7 1.0
C E:ILE110 4.3 29.9 1.0
NH2 E:ARG147 4.3 34.1 1.0
CA E:ILE109 4.4 28.8 1.0
CB E:THR111 4.5 30.0 1.0
CA E:THR111 4.7 29.6 1.0
CD1 E:ILE110 4.7 25.9 1.0
CZ E:ARG147 4.8 36.7 1.0
CG2 E:ILE110 4.9 28.6 1.0
CB E:ILE109 4.9 28.5 1.0

Chlorine binding site 6 out of 6 in 1nsl

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Chlorine binding site 6 out of 6 in the Crystal Structure of Probable Acetyltransferase


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 Probable Acetyltransferase within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Cl184

b:86.7
occ:1.00
OG1 F:THR111 2.9 30.3 1.0
CA F:GLY108 3.4 33.1 1.0
C F:GLY108 3.7 31.9 1.0
N F:THR111 3.7 31.1 1.0
N F:GLY108 3.9 33.4 1.0
CB F:THR111 4.0 31.5 1.0
NH2 F:ARG147 4.0 43.6 1.0
N F:ILE110 4.0 30.5 1.0
N F:ILE109 4.0 31.3 1.0
O F:GLY108 4.2 32.0 1.0
CB F:ILE110 4.2 30.6 1.0
CZ F:ARG147 4.4 42.9 1.0
NH1 F:ARG147 4.4 43.0 1.0
CA F:THR111 4.5 31.4 1.0
CA F:ILE110 4.5 31.3 1.0
C F:ILE110 4.6 31.5 1.0
C F:ILE109 4.8 30.9 1.0
CG2 F:VAL144 4.9 24.6 1.0
CG1 F:ILE110 4.9 29.6 1.0
CA F:ILE109 5.0 30.7 1.0

Reference:

J.S.Brunzelle, R.Wu, S.V.Korolev, F.R.Collart, A.Joachimiak, W.F.Anderson. Crystal Structure of Bacillus Subtilis Ydaf Protein: A Putative Ribosomal N-Acetyltransferase Proteins V. 57 850 2004.
ISSN: ISSN 0887-3585
PubMed: 15468321
DOI: 10.1002/PROT.10601
Page generated: Sat Dec 12 08:43:56 2020

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