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Strontium in PDB 5c02: Influenza A M2 Transmembrane Domain Drug-Resistant S31N Mutant at pH 8.0

Protein crystallography data

The structure of Influenza A M2 Transmembrane Domain Drug-Resistant S31N Mutant at pH 8.0, PDB code: 5c02 was solved by J.L.Thomaston, W.F.Degrado, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 17.84 / 1.59
Space group I 4
Cell size a, b, c (Å), α, β, γ (°) 28.650, 28.650, 68.380, 90.00, 90.00, 90.00
R / Rfree (%) 16 / 19.7

Other elements in 5c02:

The structure of Influenza A M2 Transmembrane Domain Drug-Resistant S31N Mutant at pH 8.0 also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms
Calcium (Ca) 1 atom

Strontium Binding Sites:

The binding sites of Strontium atom in the Influenza A M2 Transmembrane Domain Drug-Resistant S31N Mutant at pH 8.0 (pdb code 5c02). This binding sites where shown within 5.0 Angstroms radius around Strontium atom.
In total only one binding site of Strontium was determined in the Influenza A M2 Transmembrane Domain Drug-Resistant S31N Mutant at pH 8.0, PDB code: 5c02:

Strontium binding site 1 out of 1 in 5c02

Go back to Strontium Binding Sites List in 5c02
Strontium binding site 1 out of 1 in the Influenza A M2 Transmembrane Domain Drug-Resistant S31N Mutant at pH 8.0


Mono view


Stereo pair view

A full contact list of Strontium with other atoms in the Sr binding site number 1 of Influenza A M2 Transmembrane Domain Drug-Resistant S31N Mutant at pH 8.0 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Sr101

b:8.5
occ:0.20
O A:SER22 2.4 13.1 1.0
O A:HOH205 2.4 15.0 1.0
C A:SER22 3.5 14.0 1.0
H A:SER22 3.6 17.3 1.0
HA A:SER23 3.7 15.5 1.0
N A:SER22 4.2 14.4 1.0
OG A:SER22 4.3 18.7 1.0
N A:SER23 4.4 15.4 1.0
CA A:SER22 4.4 13.8 1.0
CA A:SER23 4.5 12.9 1.0
HG A:SER23 4.9 14.5 1.0
HG A:SER22 4.9 22.4 1.0
O A:HOH211 4.9 41.4 1.0
CB A:SER22 4.9 19.0 1.0

Reference:

J.L.Thomaston, W.F.Degrado. Crystal Structure of the Drug-Resistant S31N Influenza M2 Proton Channel. Protein Sci. V. 25 1551 2016.
ISSN: ESSN 1469-896X
PubMed: 27082171
DOI: 10.1002/PRO.2937
Page generated: Wed Dec 16 02:24:31 2020

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