Chlorine in PDB 1rxi: PI258 Arsenate Reductase (Arsc) Triple Mutant C10S/C15A/C82S

All present enzymatic activity of PI258 Arsenate Reductase (Arsc) Triple Mutant C10S/C15A/C82S:
1.20.4.1;

The structure of PI258 Arsenate Reductase (Arsc) Triple Mutant C10S/C15A/C82S, PDB code: 1rxi was solved by J.Messens, I.Van Molle, P.Vanhaesebrouck, M.Limbourg, K.Vanbelle, K.Wahni, J.C.Martins, R.Loris, L.Wyns, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	23.90 / 1.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	32.034, 34.064, 63.355, 90.00, 97.33, 90.00
R / Rfree (%)	20.9 / 23.1

The structure of PI258 Arsenate Reductase (Arsc) Triple Mutant C10S/C15A/C82S also contains other interesting chemical elements:

Potassium

(K)

1 atom

The binding sites of Chlorine atom in the PI258 Arsenate Reductase (Arsc) Triple Mutant C10S/C15A/C82S (pdb code 1rxi). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the PI258 Arsenate Reductase (Arsc) Triple Mutant C10S/C15A/C82S, PDB code: 1rxi:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the PI258 Arsenate Reductase (Arsc) Triple Mutant C10S/C15A/C82S


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of PI258 Arsenate Reductase (Arsc) Triple Mutant C10S/C15A/C82S within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl152 b:13.1 occ:1.00 CL A:LCP152 0.0 13.1 1.0 O3 A:LCP152 1.5 10.9 1.0 O2 A:LCP152 1.5 14.0 1.0 O1 A:LCP152 1.5 11.5 1.0 O4 A:LCP152 1.5 15.8 1.0 O A:GLY12 3.5 18.3 1.0 OG A:SER10 3.5 14.9 1.0 N A:ALA15 3.6 13.0 1.0 N A:ARG16 3.6 10.3 1.0 O A:HOH203 3.6 15.1 1.0 NE A:ARG16 3.7 9.2 1.0 O A:HOH254 3.7 24.5 1.0 C A:GLY12 3.8 14.3 1.0 CB A:SER10 3.9 9.7 1.0 NH2 A:ARG16 3.9 11.3 1.0 N A:GLY12 3.9 11.8 1.0 N A:SER14 4.0 11.9 1.0 CB A:ARG16 4.1 7.4 1.0 CA A:GLY12 4.2 17.5 1.0 N A:SER17 4.3 10.1 1.0 CA A:ALA15 4.3 11.2 1.0 CZ A:ARG16 4.3 9.3 1.0 C A:ALA15 4.3 11.1 1.0 OG A:SER17 4.3 17.5 1.0 CA A:ARG16 4.3 9.4 1.0 CB A:ALA15 4.4 11.7 1.0 CG A:ARG16 4.6 8.6 1.0 N A:ASN13 4.6 17.5 1.0 C A:SER14 4.6 13.0 1.0 CA A:SER14 4.6 11.4 1.0 N A:THR11 4.7 12.1 1.0 CD A:ARG16 4.7 9.2 1.0 O A:HOH269 4.7 24.2 1.0 CB A:SER14 4.8 16.9 0.5 CB A:SER14 4.8 16.2 0.5 C A:ARG16 4.9 11.1 1.0 CA A:ASN13 4.9 14.2 1.0 C A:ASN13 5.0 13.1 1.0

Chlorine binding site 2 out of 2 in the PI258 Arsenate Reductase (Arsc) Triple Mutant C10S/C15A/C82S


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of PI258 Arsenate Reductase (Arsc) Triple Mutant C10S/C15A/C82S within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl153 b:63.4 occ:1.00 O A:HOH273 3.9 36.2 1.0 N A:GLY31 3.9 23.6 1.0 O A:HOH282 4.0 24.6 1.0 O A:HOH363 4.2 36.2 1.0 O A:LEU28 4.2 19.9 1.0 CD1 A:TRP32 4.2 16.0 1.0 CA A:GLY31 4.3 20.6 1.0 CA A:LEU28 4.4 19.8 1.0 C A:LEU28 4.5 20.4 1.0 NE1 A:TRP32 4.5 17.6 1.0 O A:ILE27 4.6 21.7 1.0 CB A:GLU30 4.6 23.9 1.0 CG A:LYS129 4.6 26.7 1.0 O A:HOH264 4.7 26.1 1.0 CD2 A:LEU28 4.7 19.6 1.0 CD A:LYS129 4.8 31.7 1.0 C A:GLU30 4.9 24.4 1.0 CB A:LEU28 5.0 16.1 1.0 N A:GLU30 5.0 23.1 1.0

J.Messens, I.Van Molle, P.Vanhaesebrouck, K.Van Belle, K.Wahni, J.C.Martins, L.Wyns, R.Loris. The Structure of A Triple Mutant of PI258 Arsenate Reductase From Staphylococcus Aureus and Its 5-Thio-2-Nitrobenzoic Acid Adduct. Acta Crystallogr.,Sect.D V. 60 1180 2004.
ISSN: ISSN 0907-4449
PubMed: 15159594
DOI: 10.1107/S0907444904007334