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Chlorine in PDB 5euu: Rat Prestin Stas Domain in Complex with Chloride

Protein crystallography data

The structure of Rat Prestin Stas Domain in Complex with Chloride, PDB code: 5euu was solved by G.Lolli, E.Pasqualetto, E.Costanzi, G.Bonetto, R.Battistutta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 31.07 / 1.87
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 62.133, 62.133, 66.587, 90.00, 90.00, 120.00
R / Rfree (%) 15.7 / 19.6

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Rat Prestin Stas Domain in Complex with Chloride (pdb code 5euu). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Rat Prestin Stas Domain in Complex with Chloride, PDB code: 5euu:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 5euu

Go back to Chlorine Binding Sites List in 5euu
Chlorine binding site 1 out of 2 in the Rat Prestin Stas Domain in Complex with Chloride


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Rat Prestin Stas Domain in Complex with Chloride within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl801

b:40.4
occ:1.00
HA3 A:GLY656 2.5 30.6 1.0
H A:ASP653 2.6 34.8 1.0
HA A:MET652 2.9 27.2 1.0
O A:HOH949 3.0 41.4 1.0
HE2 A:TYR545 3.2 0.1 1.0
HB3 A:MET652 3.3 24.8 1.0
N A:ASP653 3.4 29.0 1.0
HG2 A:MET652 3.4 24.5 1.0
CA A:GLY656 3.5 25.5 1.0
HB3 A:PRO543 3.5 39.2 1.0
CA A:MET652 3.6 22.7 1.0
HE3 A:MET652 3.6 32.6 1.0
HG22 A:ILE544 3.7 50.1 1.0
HE2 A:MET652 3.7 32.6 1.0
H A:ILE544 3.7 33.5 1.0
H A:GLY656 3.8 34.2 1.0
CB A:MET652 3.8 20.7 1.0
OD1 A:ASP653 3.8 46.0 1.0
CG A:ASP653 3.9 51.6 1.0
OD2 A:ASP653 3.9 37.7 1.0
HA2 A:GLY656 3.9 30.6 1.0
CE2 A:TYR545 3.9 96.8 1.0
C A:MET652 4.0 31.4 1.0
CG A:MET652 4.0 20.4 1.0
HA A:PRO543 4.1 38.6 1.0
CE A:MET652 4.1 27.2 1.0
N A:GLY656 4.1 28.5 1.0
O A:ASP653 4.2 26.8 1.0
HH A:TYR545 4.2 67.0 1.0
HD2 A:TYR545 4.3 0.3 1.0
C A:GLY656 4.4 26.4 1.0
CB A:PRO543 4.4 32.7 1.0
CA A:ASP653 4.4 31.7 1.0
N A:ILE544 4.5 27.9 1.0
CD2 A:TYR545 4.5 88.5 1.0
O A:PHE651 4.6 22.0 1.0
CA A:PRO543 4.6 32.1 1.0
CG2 A:ILE544 4.6 41.8 1.0
CB A:ASP653 4.7 32.6 1.0
H A:VAL657 4.7 31.1 1.0
HB2 A:MET652 4.7 24.8 1.0
C A:ASP653 4.7 39.1 1.0
CZ A:TYR545 4.7 56.9 1.0
OH A:TYR545 4.8 55.9 1.0
HG3 A:MET652 4.8 24.5 1.0
N A:VAL657 4.8 25.9 1.0
N A:MET652 4.9 22.2 1.0
HB3 A:ASP653 4.9 39.2 1.0
HG21 A:ILE544 4.9 50.1 1.0
HE1 A:MET652 4.9 32.6 1.0
HB2 A:PRO543 4.9 39.2 1.0
HG3 A:PRO543 5.0 39.2 1.0
SD A:MET652 5.0 29.1 1.0

Chlorine binding site 2 out of 2 in 5euu

Go back to Chlorine Binding Sites List in 5euu
Chlorine binding site 2 out of 2 in the Rat Prestin Stas Domain in Complex with Chloride


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Rat Prestin Stas Domain in Complex with Chloride within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl802

b:45.7
occ:1.00
H A:ILE706 2.5 20.5 1.0
HB2 A:SER705 3.0 25.5 1.0
HG13 A:ILE706 3.1 27.9 1.0
O A:HOH972 3.2 23.6 1.0
O A:HOH970 3.3 39.7 1.0
HA A:SER705 3.4 23.1 1.0
N A:ILE706 3.4 17.1 1.0
HB A:ILE706 3.5 23.3 1.0
HD12 A:ILE706 3.5 28.4 1.0
CG1 A:ILE706 3.8 23.2 1.0
CB A:SER705 3.8 21.2 1.0
CA A:SER705 3.9 19.2 1.0
CB A:ILE706 4.0 19.4 1.0
CD1 A:ILE706 4.1 23.6 1.0
O A:HOH923 4.1 41.3 1.0
C A:SER705 4.2 20.8 1.0
HG21 A:THR647 4.2 35.0 1.0
HB3 A:SER705 4.2 25.5 1.0
CA A:ILE706 4.3 16.7 1.0
H A:HIS707 4.3 22.1 1.0
O A:HOH945 4.3 40.6 1.0
HD11 A:ILE706 4.3 28.4 1.0
O A:HOH936 4.4 41.4 1.0
HG12 A:ILE706 4.6 27.9 1.0
HG23 A:THR647 4.7 35.0 1.0
CG2 A:THR647 4.9 29.1 1.0
HD13 A:ILE706 4.9 28.4 1.0
OG A:SER705 4.9 21.5 1.0
HA A:ILE706 4.9 20.1 1.0
HD2 A:TYR520 5.0 30.8 1.0
N A:HIS707 5.0 18.5 1.0

Reference:

G.Lolli, E.Pasqualetto, E.Costanzi, G.Bonetto, R.Battistutta. The Stas Domain of Mammalian SLC26A5 Prestin Harbours An Anion-Binding Site. Biochem.J. V. 473 365 2016.
ISSN: ESSN 1470-8728
PubMed: 26635354
DOI: 10.1042/BJ20151089
Page generated: Sat Dec 12 11:42:08 2020

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