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Chlorine in PDB 5e6q: Importin Alpha Binding to XRCC1 Nls Peptide

Protein crystallography data

The structure of Importin Alpha Binding to XRCC1 Nls Peptide, PDB code: 5e6q was solved by L.C.Pedersen, T.W.Kirby, N.R.Gassman, C.E.Smith, S.A.Gabel, M.Sobhany, S.H.Wilson, R.E.London, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.41 / 2.31
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 78.668, 90.112, 100.699, 90.00, 90.00, 90.00
R / Rfree (%) 17.4 / 20.8

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Importin Alpha Binding to XRCC1 Nls Peptide (pdb code 5e6q). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Importin Alpha Binding to XRCC1 Nls Peptide, PDB code: 5e6q:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 5e6q

Go back to Chlorine Binding Sites List in 5e6q
Chlorine binding site 1 out of 2 in the Importin Alpha Binding to XRCC1 Nls Peptide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Importin Alpha Binding to XRCC1 Nls Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl603

b:58.2
occ:1.00
O B:HOH834 3.4 44.2 1.0
N B:THR349 3.5 26.7 1.0
OG1 B:THR349 3.8 46.9 1.0
CD B:LYS348 4.0 55.6 1.0
CA B:LYS348 4.0 31.0 1.0
CB B:THR349 4.1 36.2 1.0
O B:PRO347 4.1 32.0 1.0
C B:LYS348 4.3 29.5 1.0
CA B:THR349 4.4 35.7 1.0
NZ B:LYS348 4.7 74.4 1.0
CB B:LYS348 4.8 24.4 1.0
CE B:LYS348 4.9 71.5 1.0
C B:PRO347 4.9 31.0 1.0
N B:LYS348 4.9 29.4 1.0
CG B:LYS348 5.0 45.9 1.0

Chlorine binding site 2 out of 2 in 5e6q

Go back to Chlorine Binding Sites List in 5e6q
Chlorine binding site 2 out of 2 in the Importin Alpha Binding to XRCC1 Nls Peptide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Importin Alpha Binding to XRCC1 Nls Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl604

b:63.0
occ:1.00
O B:HOH832 3.2 25.4 1.0
O B:HOH841 3.3 35.8 1.0
N B:ALA195 3.4 14.6 1.0
N B:SER194 3.5 21.4 1.0
CB B:ALA195 3.6 21.4 1.0
C B:GLY193 3.9 24.7 1.0
CA B:GLY193 4.0 19.8 1.0
O B:HOH818 4.1 51.1 1.0
CA B:ALA195 4.1 25.1 1.0
CA B:SER194 4.2 21.9 1.0
C B:SER194 4.3 20.2 1.0
CB B:SER194 4.4 20.5 1.0
O B:GLY193 4.8 19.4 1.0
O B:HOH824 4.9 55.7 1.0

Reference:

T.W.Kirby, N.R.Gassman, C.E.Smith, L.C.Pedersen, S.A.Gabel, M.Sobhany, S.H.Wilson, R.E.London. Nuclear Localization of the Dna Repair Scaffold XRCC1: Uncovering the Functional Role of A Bipartite Nls. Sci Rep V. 5 13405 2015.
ISSN: ESSN 2045-2322
PubMed: 26304019
DOI: 10.1038/SREP13405
Page generated: Fri Jul 26 07:06:11 2024

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