Chlorine in PDB 1m8d: Inducible Nitric Oxide Synthase with Chlorzoxazone Bound

All present enzymatic activity of Inducible Nitric Oxide Synthase with Chlorzoxazone Bound:
1.14.13.39;

The structure of Inducible Nitric Oxide Synthase with Chlorzoxazone Bound, PDB code: 1m8d was solved by R.J.Rosenfeld, E.D.Garcin, K.Panda, G.Andersson, A.Aberg, A.V.Wallace, D.J.Stuehr, J.A.Tainer, E.D.Getzoff, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.84 / 2.35
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	213.891, 213.891, 115.484, 90.00, 90.00, 120.00
R / Rfree (%)	23.8 / 26.8

The structure of Inducible Nitric Oxide Synthase with Chlorzoxazone Bound also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Chlorine atom in the Inducible Nitric Oxide Synthase with Chlorzoxazone Bound (pdb code 1m8d). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Inducible Nitric Oxide Synthase with Chlorzoxazone Bound, PDB code: 1m8d:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Inducible Nitric Oxide Synthase with Chlorzoxazone Bound


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Inducible Nitric Oxide Synthase with Chlorzoxazone Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl906 b:42.2 occ:1.00 CL1 A:CLW906 0.0 42.2 1.0 C6 A:CLW906 1.7 35.0 1.0 C1 A:CLW906 2.7 34.3 1.0 C5 A:CLW906 2.8 32.5 1.0 CD1 A:PHE363 3.4 38.0 1.0 NC A:HEM901 3.4 30.4 1.0 C1C A:HEM901 3.4 30.9 1.0 CE1 A:PHE363 3.5 37.4 1.0 C4C A:HEM901 3.7 31.2 1.0 CA A:ASN364 3.8 33.9 1.0 N A:GLY365 3.8 33.8 1.0 C2C A:HEM901 3.8 29.5 1.0 C A:ASN364 3.9 34.1 1.0 O A:PHE363 3.9 33.1 1.0 C3C A:HEM901 4.0 27.9 1.0 CHC A:HEM901 4.0 33.9 1.0 C2 A:CLW906 4.0 34.0 1.0 CG2 A:VAL346 4.0 39.0 1.0 C4 A:CLW906 4.1 32.0 1.0 N A:ASN364 4.2 33.4 1.0 FE A:HEM901 4.3 33.6 1.0 CHD A:HEM901 4.3 32.8 1.0 O A:PRO344 4.3 38.7 1.0 C A:PHE363 4.3 34.8 1.0 ND A:HEM901 4.5 33.9 1.0 NB A:HEM901 4.5 31.7 1.0 C3 A:CLW906 4.5 35.3 1.0 C4B A:HEM901 4.5 31.6 1.0 N A:VAL346 4.5 43.2 1.0 C1D A:HEM901 4.6 33.3 1.0 CMC A:HEM901 4.6 31.0 1.0 CA A:GLY365 4.7 35.8 1.0 CG A:PHE363 4.7 38.3 1.0 O A:ASN364 4.7 31.5 1.0 CB A:VAL346 4.8 43.8 1.0 CAC A:HEM901 4.9 31.0 1.0 CZ A:PHE363 4.9 38.2 1.0

Chlorine binding site 2 out of 2 in the Inducible Nitric Oxide Synthase with Chlorzoxazone Bound


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Inducible Nitric Oxide Synthase with Chlorzoxazone Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl907 b:41.7 occ:1.00 CL1 B:CLW907 0.0 41.7 1.0 C6 B:CLW907 1.7 34.2 1.0 C1 B:CLW907 2.7 34.9 1.0 C5 B:CLW907 2.8 33.1 1.0 NC B:HEM901 3.5 32.8 1.0 C1C B:HEM901 3.5 31.7 1.0 CD1 B:PHE363 3.5 37.9 1.0 CE1 B:PHE363 3.6 37.9 1.0 C4C B:HEM901 3.7 33.2 1.0 CA B:ASN364 3.9 35.4 1.0 N B:GLY365 3.9 35.4 1.0 C2C B:HEM901 3.9 29.6 1.0 C B:ASN364 4.0 35.4 1.0 C3C B:HEM901 4.0 29.5 1.0 CG2 B:VAL346 4.0 39.2 1.0 C2 B:CLW907 4.0 35.3 1.0 CHC B:HEM901 4.1 33.9 1.0 O B:PHE363 4.1 34.9 1.0 C4 B:CLW907 4.1 32.0 1.0 O B:PRO344 4.2 39.4 1.0 CHD B:HEM901 4.2 33.1 1.0 FE B:HEM901 4.3 37.6 1.0 N B:ASN364 4.4 35.1 1.0 NB B:HEM901 4.4 30.9 1.0 ND B:HEM901 4.5 35.3 1.0 C B:PHE363 4.5 36.4 1.0 C4B B:HEM901 4.5 32.8 1.0 N B:VAL346 4.5 42.9 1.0 C3 B:CLW907 4.5 34.1 1.0 C1D B:HEM901 4.6 32.5 1.0 CA B:GLY365 4.7 37.2 1.0 CMC B:HEM901 4.7 31.7 1.0 O B:ASN364 4.8 35.6 1.0 CB B:VAL346 4.8 43.1 1.0 CG B:PHE363 4.8 36.8 1.0 C B:PRO344 4.9 39.1 1.0 CA B:ALA345 5.0 40.1 1.0 CAC B:HEM901 5.0 31.8 1.0 CZ B:PHE363 5.0 38.3 1.0

R.J.Rosenfeld, E.D.Garcin, K.Panda, G.Andersson, A.Aberg, A.V.Wallace, G.M.Morris, A.J.Olson, D.J.Stuehr, J.A.Tainer, E.D.Getzoff. Conformational Changes in Nitric Oxide Synthases Induced By Chlorzoxazone and Nitroindazoles: Crystallographic and Computational Analyses of Inhibitor Potency Biochemistry V. 41 13915 2002.
ISSN: ISSN 0006-2960
PubMed: 12437348
DOI: 10.1021/BI026313J