Chlorine in PDB 3nvr: Modulating Heme Redox Potential Through Protein-Induced Porphyrin Distortion

The structure of Modulating Heme Redox Potential Through Protein-Induced Porphyrin Distortion, PDB code: 3nvr was solved by C.Olea Jr., J.Kuriyan, M.A.Marletta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.48 / 2.15
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	79.825, 126.095, 42.742, 90.00, 90.00, 90.00
R / Rfree (%)	21.7 / 26

The structure of Modulating Heme Redox Potential Through Protein-Induced Porphyrin Distortion also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Chlorine atom in the Modulating Heme Redox Potential Through Protein-Induced Porphyrin Distortion (pdb code 3nvr). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Modulating Heme Redox Potential Through Protein-Induced Porphyrin Distortion, PDB code: 3nvr:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Modulating Heme Redox Potential Through Protein-Induced Porphyrin Distortion


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Modulating Heme Redox Potential Through Protein-Induced Porphyrin Distortion within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl189 b:0.3 occ:1.00 CE A:MET137 3.2 75.5 1.0 O A:ASP45 4.1 53.2 1.0 CG1 A:VAL48 4.1 47.0 1.0 N A:ARG49 4.3 53.3 1.0 CB A:ARG49 4.3 68.3 1.0 CA A:ARG49 4.4 61.3 1.0 CZ2 A:TRP67 4.5 38.8 1.0 CB A:VAL48 4.6 54.0 1.0 SD A:MET137 4.7 53.8 1.0 C A:VAL48 4.9 51.2 1.0 C A:ASP45 4.9 54.2 1.0 CB A:ASP45 5.0 58.6 1.0

Chlorine binding site 2 out of 2 in the Modulating Heme Redox Potential Through Protein-Induced Porphyrin Distortion


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Modulating Heme Redox Potential Through Protein-Induced Porphyrin Distortion within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl189 b:99.7 occ:1.00 O B:ASP45 3.8 60.5 1.0 O B:HOH209 3.9 43.5 1.0 N B:ARG49 4.4 47.3 1.0 CZ2 B:TRP67 4.4 35.9 1.0 CG1 B:VAL48 4.4 41.4 1.0 CA B:ARG49 4.4 48.3 1.0 CB B:ARG49 4.5 51.3 1.0 CB B:VAL48 4.8 51.7 1.0 C B:ASP45 4.9 62.4 1.0

C.Olea, J.Kuriyan, M.A.Marletta. Modulating Heme Redox Potential Through Protein-Induced Porphyrin Distortion J.Am.Chem.Soc. V. 132 12794 2010.
ISSN: ISSN 0002-7863
PubMed: 20735135
DOI: 10.1021/JA106252B