Chlorine in PDB 2iwf: Resting Form of Pink Nitrous Oxide Reductase From Achromobacter Cycloclastes

All present enzymatic activity of Resting Form of Pink Nitrous Oxide Reductase From Achromobacter Cycloclastes:
1.7.99.6;

The structure of Resting Form of Pink Nitrous Oxide Reductase From Achromobacter Cycloclastes, PDB code: 2iwf was solved by K.Paraskevopoulos, S.V.Antonyuk, R.G.Sawers, R.R.Eady, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.00 / 1.86
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	70.292, 118.180, 131.135, 90.00, 90.00, 90.00
R / Rfree (%)	20.9 / 27.1

The structure of Resting Form of Pink Nitrous Oxide Reductase From Achromobacter Cycloclastes also contains other interesting chemical elements:

Copper	(Cu)	12 atoms
Calcium	(Ca)	5 atoms
Sodium	(Na)	13 atoms

The binding sites of Chlorine atom in the Resting Form of Pink Nitrous Oxide Reductase From Achromobacter Cycloclastes (pdb code 2iwf). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Resting Form of Pink Nitrous Oxide Reductase From Achromobacter Cycloclastes, PDB code: 2iwf:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Resting Form of Pink Nitrous Oxide Reductase From Achromobacter Cycloclastes


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Resting Form of Pink Nitrous Oxide Reductase From Achromobacter Cycloclastes within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1608 b:19.1 occ:1.00 O A:HOH2143 3.0 35.3 1.0 NH1 A:ARG145 3.1 21.4 1.0 ND1 A:HIS340 3.2 20.1 1.0 ND2 A:ASN288 3.2 22.7 1.0 CE1 A:HIS340 3.4 21.7 1.0 NH2 A:ARG145 3.4 23.4 1.0 N A:CYS287 3.4 20.5 1.0 CB A:ASN204 3.7 21.9 1.0 CZ A:ARG145 3.7 22.6 1.0 CA A:GLY286 3.7 19.4 1.0 CG A:ASN204 3.7 22.2 1.0 O A:CYS287 4.0 22.3 1.0 OD1 A:ASN204 4.1 25.2 1.0 CG A:ASN288 4.1 20.6 1.0 O A:HOH2269 4.1 16.5 1.0 C A:GLY286 4.1 20.0 1.0 ND2 A:ASN204 4.2 18.3 1.0 OD1 A:ASN288 4.2 21.4 1.0 CE1 A:HIS391 4.3 21.8 1.0 C A:CYS287 4.3 21.1 1.0 CA A:CYS287 4.4 21.5 1.0 CG A:HIS340 4.5 20.8 1.0 O A:HOH2144 4.5 19.5 1.0 NE2 A:HIS340 4.7 24.2 1.0 ND1 A:HIS391 4.8 19.7 1.0 CB A:CYS287 4.9 21.9 1.0 N A:GLY286 4.9 18.8 1.0 O A:HOH2070 5.0 30.6 1.0 CA A:ASN204 5.0 22.0 1.0

Chlorine binding site 2 out of 2 in the Resting Form of Pink Nitrous Oxide Reductase From Achromobacter Cycloclastes


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Resting Form of Pink Nitrous Oxide Reductase From Achromobacter Cycloclastes within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1607 b:21.5 occ:1.00 NH1 B:ARG145 3.1 27.8 1.0 ND2 B:ASN288 3.3 24.8 1.0 ND1 B:HIS340 3.3 25.3 1.0 N B:CYS287 3.5 22.5 1.0 NH2 B:ARG145 3.5 25.8 1.0 CB B:ASN204 3.5 23.0 1.0 CG B:ASN204 3.6 24.6 1.0 CA B:GLY286 3.7 23.0 1.0 O B:HOH2067 3.7 32.7 1.0 CZ B:ARG145 3.8 25.7 1.0 CE1 B:HIS340 3.8 27.5 1.0 OD1 B:ASN204 3.9 28.9 1.0 CG B:ASN288 4.0 19.7 1.0 OD1 B:ASN288 4.0 22.8 1.0 O B:CYS287 4.1 21.6 1.0 O B:HOH2244 4.1 22.5 1.0 C B:GLY286 4.1 22.6 1.0 ND2 B:ASN204 4.2 25.6 1.0 C B:CYS287 4.3 21.0 1.0 CE1 B:HIS391 4.4 21.4 1.0 CA B:CYS287 4.5 22.5 1.0 O B:HOH2144 4.5 15.6 1.0 CG B:HIS340 4.6 24.5 1.0 N B:GLY286 4.7 23.4 1.0 ND1 B:HIS391 4.8 17.8 1.0 CB B:CYS287 4.9 22.8 1.0 CA B:ASN204 4.9 23.0 1.0 O B:HIS285 5.0 24.3 1.0

K.Paraskevopoulos, S.V.Antonyuk, R.G.Sawers, R.R.Eady, S.S.Hasnain. Insight Into Catalysis of Nitrous Oxide Reductase From High-Resolution Structures of Resting and Inhibitor-Bound Enzyme From Achromobacter Cycloclastes. J.Mol.Biol. V. 362 55 2006.
ISSN: ISSN 0022-2836
PubMed: 16904686
DOI: 10.1016/J.JMB.2006.06.064