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Sodium in PDB 5w7w: Crystal Structure of Fha Domain of Human Aplf

Enzymatic activity of Crystal Structure of Fha Domain of Human Aplf

All present enzymatic activity of Crystal Structure of Fha Domain of Human Aplf:
4.2.99.18;

Protein crystallography data

The structure of Crystal Structure of Fha Domain of Human Aplf, PDB code: 5w7w was solved by L.C.Pedersen, K.Kim, R.E.London, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.27 / 1.35
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 56.794, 96.944, 34.696, 90.00, 90.00, 90.00
R / Rfree (%) 14.7 / 16.4

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Fha Domain of Human Aplf (pdb code 5w7w). 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 Fha Domain of Human Aplf, PDB code: 5w7w:

Sodium binding site 1 out of 1 in 5w7w

Go back to Sodium Binding Sites List in 5w7w
Sodium binding site 1 out of 1 in the Crystal Structure of Fha Domain of Human Aplf


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 Fha Domain of Human Aplf within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na202

b:24.4
occ:1.00
O A:MET1 2.2 18.1 1.0
O A:HOH365 2.2 32.8 1.0
O A:HOH319 2.6 25.8 1.0
O A:HOH386 3.2 34.7 1.0
H A:MET1 3.2 22.1 1.0
C A:MET1 3.4 16.2 1.0
HA A:SER2 3.8 23.3 1.0
N A:MET1 3.9 18.4 1.0
H A:GLY3 4.1 24.8 1.0
HG2 A:MET1 4.2 20.0 1.0
CA A:MET1 4.3 18.2 1.0
N A:SER2 4.4 18.1 1.0
O A:GLY3 4.4 23.4 1.0
CA A:SER2 4.5 19.4 1.0
HG3 A:MET1 4.5 20.0 1.0
N A:GLY3 4.6 20.6 1.0
O1 A:FMT201 4.7 26.2 1.0
CG A:MET1 4.8 16.7 1.0
C A:SER2 4.8 20.8 1.0
C A:THR0 5.0 16.1 1.0

Reference:

K.Kim, L.C.Pedersen, T.W.Kirby, E.F.Derose, R.E.London. Characterization of the Aplf Fha-XRCC1 Phosphopeptide Interaction and Its Structural and Functional Implications. Nucleic Acids Res. V. 45 12374 2017.
ISSN: ESSN 1362-4962
PubMed: 29059378
DOI: 10.1093/NAR/GKX941
Page generated: Tue Dec 15 11:47:20 2020

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