Atomistry » Chlorine » PDB 3lcd-3lnr » 3lda
Atomistry »
  Chlorine »
    PDB 3lcd-3lnr »
      3lda »

Chlorine in PDB 3lda: Yeast RAD51 H352Y Filament Interface Mutant

Protein crystallography data

The structure of Yeast RAD51 H352Y Filament Interface Mutant, PDB code: 3lda was solved by N.L.Villanueva, J.Chen, S.W.Morrical, M.A.Rould, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.50
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 78.905, 78.905, 130.333, 90.00, 90.00, 120.00
R / Rfree (%) 20 / 24.6

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Yeast RAD51 H352Y Filament Interface Mutant (pdb code 3lda). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Yeast RAD51 H352Y Filament Interface Mutant, PDB code: 3lda:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in 3lda

Go back to Chlorine Binding Sites List in 3lda
Chlorine binding site 1 out of 3 in the Yeast RAD51 H352Y Filament Interface Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Yeast RAD51 H352Y Filament Interface Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1080

b:42.8
occ:1.00
NE A:ARG154 3.3 31.4 1.0
CD A:ARG154 3.7 32.3 1.0
CD2 A:HIS151 3.8 48.1 1.0
NE2 A:HIS151 4.4 50.9 1.0
CZ A:ARG154 4.4 31.5 1.0
CG A:HIS151 4.4 45.1 1.0
CB A:ARG154 4.6 34.7 1.0
CA A:HIS151 4.6 35.8 1.0
NH1 A:ARG154 4.7 30.3 1.0
CG A:ARG154 4.8 32.9 1.0
CB A:HIS151 4.9 39.4 1.0

Chlorine binding site 2 out of 3 in 3lda

Go back to Chlorine Binding Sites List in 3lda
Chlorine binding site 2 out of 3 in the Yeast RAD51 H352Y Filament Interface Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Yeast RAD51 H352Y Filament Interface Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1081

b:64.2
occ:1.00
N A:LYS191 3.3 34.9 1.0
CB A:LYS191 3.3 32.9 1.0
N A:ARG188 3.4 45.8 1.0
NZ A:LYS191 3.4 41.3 1.0
N A:THR189 3.4 41.1 1.0
N A:SER192 3.5 36.2 1.0
CE A:LYS191 3.7 35.9 1.0
CA A:LYS191 3.7 35.1 1.0
N A:GLY190 3.8 37.6 1.0
CG A:LYS191 3.9 32.8 1.0
OG1 A:THR189 3.9 40.1 1.0
CA A:ARG188 3.9 45.2 1.0
O A:GLU186 4.0 43.3 1.0
C A:ARG188 4.1 43.5 1.0
C A:LYS191 4.2 35.9 1.0
C A:GLY190 4.2 36.3 1.0
C A:PHE187 4.2 46.0 1.0
CA A:PHE187 4.3 46.8 1.0
CA A:THR189 4.3 39.6 1.0
C A:THR189 4.4 38.0 1.0
CB A:SER192 4.4 39.6 1.0
CD A:LYS191 4.4 34.7 1.0
CA A:GLY190 4.5 36.7 1.0
CA A:SER192 4.6 36.9 1.0
CB A:THR189 4.8 39.7 1.0
OE1 A:GLN326 4.8 62.6 1.0
C A:GLU186 5.0 43.0 1.0

Chlorine binding site 3 out of 3 in 3lda

Go back to Chlorine Binding Sites List in 3lda
Chlorine binding site 3 out of 3 in the Yeast RAD51 H352Y Filament Interface Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Yeast RAD51 H352Y Filament Interface Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1082

b:62.9
occ:1.00
O A:ARG188 3.1 44.8 1.0
N A:GLY190 3.2 37.6 1.0
C A:ARG188 3.2 43.5 1.0
NH1 A:ARG368 3.5 39.9 1.0
NE A:ARG368 3.5 43.1 1.0
CA A:ARG188 3.5 45.2 1.0
CA A:GLY190 3.7 36.7 1.0
CG A:ARG188 3.7 47.1 0.5
N A:THR189 3.8 41.1 1.0
CZ A:ARG368 4.0 42.1 1.0
C A:THR189 4.1 38.0 1.0
CB A:ARG188 4.2 46.6 1.0
CA A:THR189 4.4 39.6 1.0
CG A:GLN193 4.4 37.6 1.0
CD A:ARG368 4.7 40.6 1.0
NH2 A:ARG188 4.7 49.8 0.5
N A:ARG188 4.7 45.8 1.0
CG1 A:ILE387 4.7 43.0 1.0
C A:GLY190 4.8 36.3 1.0

Reference:

J.Chen, N.Villanueva, M.A.Rould, S.W.Morrical. Insights Into the Mechanism of RAD51 Recombinase From the Structure and Properties of A Filament Interface Mutant. Nucleic Acids Res. V. 38 4889 2010.
ISSN: ISSN 0305-1048
PubMed: 20371520
DOI: 10.1093/NAR/GKQ209
Page generated: Fri Jul 11 07:26:22 2025

Last articles

Cl in 3W82
Cl in 3W96
Cl in 3W81
Cl in 3W8F
Cl in 3W8D
Cl in 3W7V
Cl in 3W5F
Cl in 3W78
Cl in 3W7R
Cl in 3W6X
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy