Atomistry » Sodium » PDB 1evr-1gb5 » 1ewn
Atomistry »
  Sodium »
    PDB 1evr-1gb5 »
      1ewn »

Sodium in PDB 1ewn: Crystal Structure of the Human Aag Dna Repair Glycosylase Complexed with 1,N6-Ethenoadenine-Dna

Enzymatic activity of Crystal Structure of the Human Aag Dna Repair Glycosylase Complexed with 1,N6-Ethenoadenine-Dna

All present enzymatic activity of Crystal Structure of the Human Aag Dna Repair Glycosylase Complexed with 1,N6-Ethenoadenine-Dna:
3.2.2.21;

Protein crystallography data

The structure of Crystal Structure of the Human Aag Dna Repair Glycosylase Complexed with 1,N6-Ethenoadenine-Dna, PDB code: 1ewn was solved by A.Y.Lau, M.D.Wyatt, B.J.Glassner, L.D.Samson, T.Ellenberger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 500.00 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 42.145, 57.336, 125.517, 90.00, 90.00, 90.00
R / Rfree (%) 23 / 25.9

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of the Human Aag Dna Repair Glycosylase Complexed with 1,N6-Ethenoadenine-Dna (pdb code 1ewn). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of the Human Aag Dna Repair Glycosylase Complexed with 1,N6-Ethenoadenine-Dna, PDB code: 1ewn:

Sodium binding site 1 out of 1 in 1ewn

Go back to Sodium Binding Sites List in 1ewn
Sodium binding site 1 out of 1 in the Crystal Structure of the Human Aag Dna Repair Glycosylase Complexed with 1,N6-Ethenoadenine-Dna


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of the Human Aag Dna Repair Glycosylase Complexed with 1,N6-Ethenoadenine-Dna within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na501

b:34.2
occ:1.00
O A:SER172 2.4 33.2 1.0
O A:ALA177 2.4 28.5 1.0
O A:GLY174 2.4 39.5 1.0
OG A:SER171 2.5 29.6 1.0
O A:MET149 2.5 36.0 1.0
O A:HOH541 2.6 36.4 1.0
N A:SER172 3.3 29.4 1.0
C A:SER172 3.5 33.0 1.0
C A:ALA177 3.5 28.9 1.0
C A:GLY174 3.6 39.1 1.0
C A:MET149 3.6 36.7 1.0
N A:ALA177 3.6 30.3 1.0
CB A:SER171 3.7 26.1 1.0
CA A:ALA177 4.0 29.1 1.0
CA A:SER171 4.0 26.5 1.0
C A:SER171 4.0 26.6 1.0
CA A:SER172 4.1 30.6 1.0
O A:MET151 4.1 37.9 1.0
N A:GLY176 4.1 36.0 1.0
CB A:ALA177 4.3 29.0 1.0
N A:GLY174 4.3 36.7 1.0
CA A:MET149 4.4 36.1 1.0
C A:GLN173 4.4 36.9 1.0
CA A:ASP175 4.4 40.3 1.0
N A:ASP175 4.5 38.9 1.0
OG A:SER172 4.5 29.3 1.0
CA A:GLY174 4.5 37.8 1.0
C A:GLY176 4.6 33.3 1.0
O A:GLN173 4.6 36.9 1.0
C A:ASP175 4.6 38.8 1.0
N A:GLN173 4.6 35.0 1.0
N A:PHE150 4.6 37.3 1.0
N A:CYS178 4.7 26.4 1.0
CA A:PHE150 4.8 37.5 1.0
CA A:GLN173 4.9 36.6 1.0
CA A:GLY176 4.9 34.0 1.0
CB A:SER172 4.9 30.5 1.0

Reference:

A.Y.Lau, M.D.Wyatt, B.J.Glassner, L.D.Samson, T.Ellenberger. Molecular Basis For Discriminating Between Normal and Damaged Bases By the Human Alkyladenine Glycosylase, Aag. Proc.Natl.Acad.Sci.Usa V. 97 13573 2000.
ISSN: ISSN 0027-8424
PubMed: 11106395
DOI: 10.1073/PNAS.97.25.13573
Page generated: Sun Oct 6 18:27:30 2024

Last articles

Fe in 2YXO
Fe in 2YRS
Fe in 2YXC
Fe in 2YNM
Fe in 2YVJ
Fe in 2YP1
Fe in 2YU2
Fe in 2YU1
Fe in 2YQB
Fe in 2YOO
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy