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Chlorine in PDB 2i0q: Crystal Structure of A Telomere Single-Strand Dna-Protein Complex From O. Nova with Full-Length Alpha and Beta Telomere Proteins

Protein crystallography data

The structure of Crystal Structure of A Telomere Single-Strand Dna-Protein Complex From O. Nova with Full-Length Alpha and Beta Telomere Proteins, PDB code: 2i0q was solved by M.P.Horvath, P.Buczek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.91
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 93.331, 93.331, 423.779, 90.00, 90.00, 120.00
R / Rfree (%) 24.3 / 26.4

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of A Telomere Single-Strand Dna-Protein Complex From O. Nova with Full-Length Alpha and Beta Telomere Proteins (pdb code 2i0q). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Crystal Structure of A Telomere Single-Strand Dna-Protein Complex From O. Nova with Full-Length Alpha and Beta Telomere Proteins, PDB code: 2i0q:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 2i0q

Go back to Chlorine Binding Sites List in 2i0q
Chlorine binding site 1 out of 4 in the Crystal Structure of A Telomere Single-Strand Dna-Protein Complex From O. Nova with Full-Length Alpha and Beta Telomere Proteins


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 A Telomere Single-Strand Dna-Protein Complex From O. Nova with Full-Length Alpha and Beta Telomere Proteins within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl496

b:36.6
occ:1.00
OG1 A:THR157 3.0 31.7 1.0
O A:HOH572 3.2 31.6 1.0
N A:THR157 3.3 32.4 1.0
O A:HOH709 3.5 50.8 1.0
CB A:THR157 3.6 32.4 1.0
O A:HOH560 3.7 30.4 1.0
CE1 A:PHE172 3.8 29.7 1.0
CB A:VAL156 3.8 32.0 1.0
N A:VAL156 3.8 33.6 1.0
CD2 A:HIS114 3.9 19.9 1.0
O A:HOH616 3.9 52.7 1.0
CA A:THR157 4.1 32.9 1.0
CA A:VAL156 4.2 33.1 1.0
OG A:SER155 4.2 30.9 1.0
CB A:SER155 4.2 30.9 1.0
CD1 A:PHE172 4.2 30.6 1.0
C A:VAL156 4.2 33.9 1.0
CZ A:PHE172 4.5 27.6 1.0
C A:SER155 4.6 33.5 1.0
CG A:HIS114 4.7 19.7 1.0
CG1 A:VAL156 4.7 31.8 1.0
CG2 A:VAL156 4.7 31.6 1.0
CB A:HIS114 4.8 23.9 1.0
O A:HOH525 4.8 28.8 1.0
CA A:SER155 5.0 32.9 1.0
NE2 A:HIS114 5.0 20.9 1.0

Chlorine binding site 2 out of 4 in 2i0q

Go back to Chlorine Binding Sites List in 2i0q
Chlorine binding site 2 out of 4 in the Crystal Structure of A Telomere Single-Strand Dna-Protein Complex From O. Nova with Full-Length Alpha and Beta Telomere Proteins


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 A Telomere Single-Strand Dna-Protein Complex From O. Nova with Full-Length Alpha and Beta Telomere Proteins within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl497

b:36.5
occ:1.00
CE B:LYS182 3.0 47.9 1.0
NE A:ARG481 3.3 34.2 1.0
N A:GLY484 3.3 32.1 1.0
N B:GLY183 3.5 35.0 1.0
NZ B:LYS182 3.5 46.2 1.0
N A:ASN483 3.6 33.6 1.0
O B:GLY183 3.7 34.8 1.0
CA A:ASN483 3.8 32.8 1.0
NH2 A:ARG481 3.8 34.8 1.0
CZ A:ARG481 4.0 37.4 1.0
C A:ASN483 4.0 32.0 1.0
CA B:LYS182 4.0 39.1 1.0
O B:HOH431 4.1 55.4 1.0
CD A:ARG481 4.1 36.4 1.0
CG A:ARG481 4.2 34.1 1.0
CA A:GLY484 4.2 31.1 1.0
C B:LYS182 4.3 36.6 1.0
CD B:LYS182 4.3 45.7 1.0
CA B:GLY183 4.4 33.6 1.0
C A:ARG482 4.5 33.6 1.0
C B:GLY183 4.5 33.3 1.0
O B:LYS181 4.5 42.3 1.0
CG B:LYS182 4.6 44.1 1.0
CB B:LYS182 4.7 40.6 1.0
CA A:ARG482 4.9 35.9 1.0

Chlorine binding site 3 out of 4 in 2i0q

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Chlorine binding site 3 out of 4 in the Crystal Structure of A Telomere Single-Strand Dna-Protein Complex From O. Nova with Full-Length Alpha and Beta Telomere Proteins


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 A Telomere Single-Strand Dna-Protein Complex From O. Nova with Full-Length Alpha and Beta Telomere Proteins within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl498

b:37.9
occ:1.00
O A:HOH635 3.0 39.3 1.0
NH1 B:ARG152 3.2 33.9 1.0
O A:HOH711 3.2 45.8 1.0
NE2 A:GLN423 3.3 30.5 1.0
CG B:GLN149 3.6 32.2 1.0
CA B:GLN149 3.7 32.2 1.0
CD B:ARG152 3.7 31.2 1.0
CB B:ARG152 3.8 33.1 1.0
CB B:GLN149 3.8 32.0 1.0
CG A:GLN423 3.8 30.6 1.0
O B:GLN149 4.1 31.9 1.0
CD A:GLN423 4.1 33.9 1.0
CG B:ARG152 4.2 33.5 1.0
CZ B:ARG152 4.2 30.9 1.0
CD B:GLN149 4.4 33.6 1.0
C B:GLN149 4.4 33.1 1.0
O A:HOH653 4.4 42.1 1.0
NE B:ARG152 4.4 29.6 1.0
OH A:TYR374 4.8 32.2 1.0
N B:GLN149 4.8 30.2 1.0
O A:HOH588 4.9 40.0 1.0
NE2 B:GLN149 4.9 31.8 1.0
OE1 B:GLN149 4.9 33.4 1.0
O A:HOH637 5.0 42.5 1.0

Chlorine binding site 4 out of 4 in 2i0q

Go back to Chlorine Binding Sites List in 2i0q
Chlorine binding site 4 out of 4 in the Crystal Structure of A Telomere Single-Strand Dna-Protein Complex From O. Nova with Full-Length Alpha and Beta Telomere Proteins


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 A Telomere Single-Strand Dna-Protein Complex From O. Nova with Full-Length Alpha and Beta Telomere Proteins within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl499

b:40.4
occ:1.00
OG1 A:THR126 3.1 37.6 1.0
ND2 A:ASN137 3.1 32.8 1.0
O A:HOH571 3.3 42.1 1.0
CD A:ARG128 3.5 34.5 1.0
CB A:THR126 3.7 35.2 1.0
CG A:ARG128 3.8 33.8 1.0
CB A:ARG128 3.9 33.0 1.0
CG A:ASN137 4.0 35.4 1.0
C A:THR126 4.0 37.0 1.0
CB A:ASN137 4.1 31.9 1.0
O A:THR126 4.1 35.4 1.0
C A:LEU127 4.1 36.0 1.0
N A:LEU127 4.2 34.8 1.0
N A:ARG128 4.3 33.2 1.0
O A:LEU127 4.3 33.5 1.0
CA A:LEU127 4.5 34.6 1.0
CA A:THR126 4.5 35.2 1.0
NE A:ARG128 4.6 34.1 1.0
CA A:ARG128 4.7 32.2 1.0
NH1 A:ARG128 4.7 29.9 1.0
O A:GLN135 4.8 30.3 1.0
O A:HOH737 4.9 54.1 1.0
CG2 A:THR126 5.0 36.8 1.0
N A:ASN137 5.0 30.4 1.0

Reference:

P.Buczek, M.P.Horvath. Structural Reorganization and the Cooperative Binding of Single-Stranded Telomere Dna in Sterkiella Nova. J.Biol.Chem. V. 281 40124 2006.
ISSN: ISSN 0021-9258
PubMed: 17082188
DOI: 10.1074/JBC.M607749200
Page generated: Sat Jul 20 08:00:06 2024

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