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Sodium in PDB 1f4r: 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:
3.2.2.20;

Protein crystallography data

The structure of Crystal Structure of the Human Aag Dna Repair Glycosylase Complexed with 1,N6-Ethenoadenine-Dna, PDB code: 1f4r 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 / 2.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 42.100, 57.300, 125.500, 90.00, 90.00, 90.00
R / Rfree (%) 23.9 / 27.6

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 1f4r). 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: 1f4r:

Sodium binding site 1 out of 1 in 1f4r

Go back to Sodium Binding Sites List in 1f4r
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:Na1001

b:33.3
occ:1.00
 O A:SER172 2.3 29.6 1.0
OG A:SER171 2.4 22.9 1.0
O A:MET149 2.5 32.9 1.0
O A:ALA177 2.5 24.5 1.0
O A:GLY174 2.6 33.9 1.0
O A:HOH42 2.6 33.6 1.0
N A:SER172 3.2 26.9 1.0
C A:SER172 3.4 29.3 1.0
CB A:SER171 3.6 25.4 1.0
C A:ALA177 3.6 25.0 1.0
C A:MET149 3.7 32.5 1.0
C A:GLY174 3.7 33.6 1.0
C A:SER171 3.8 26.5 1.0
N A:ALA177 3.9 26.3 1.0
CA A:SER171 3.9 25.4 1.0
CA A:SER172 4.0 28.0 1.0
O A:MET151 4.0 31.4 1.0
CA A:ALA177 4.2 25.0 1.0
N A:GLY174 4.3 33.1 1.0
N A:GLY176 4.4 30.9 1.0
CA A:MET149 4.4 32.6 1.0
C A:GLN173 4.4 31.8 1.0
CB A:ALA177 4.5 25.8 1.0
CA A:ASP175 4.5 34.2 1.0
N A:ASP175 4.5 33.7 1.0
OG A:SER172 4.5 26.1 1.0
N A:GLN173 4.5 30.3 1.0
CA A:GLY174 4.6 32.5 1.0
N A:PHE150 4.6 32.4 1.0
O A:GLN173 4.7 32.6 1.0
N A:CYS178 4.8 24.2 1.0
CA A:PHE150 4.8 32.4 1.0
C A:ASP175 4.8 32.8 1.0
CA A:GLN173 4.9 32.1 1.0
O A:SER171 4.9 27.1 1.0
CB A:SER172 4.9 27.5 1.0
C A:GLY176 4.9 28.1 1.0
O A:GLY148 4.9 31.6 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 18:27:31 2024

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