Chlorine in PDB 5b82: Crystal Structure of the Cyanobacterial Heme-Protein TLL0287

The structure of Crystal Structure of the Cyanobacterial Heme-Protein TLL0287, PDB code: 5b82 was solved by M.Suga, T.Motomura, J.R.Shen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.62 / 2.00
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	101.246, 101.246, 33.076, 90.00, 90.00, 90.00
R / Rfree (%)	17.7 / 23.4

The structure of Crystal Structure of the Cyanobacterial Heme-Protein TLL0287 also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Chlorine atom in the Crystal Structure of the Cyanobacterial Heme-Protein TLL0287 (pdb code 5b82). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of the Cyanobacterial Heme-Protein TLL0287, PDB code: 5b82:

Chlorine binding site 1 out of 1 in the Crystal Structure of the Cyanobacterial Heme-Protein TLL0287


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the Cyanobacterial Heme-Protein TLL0287 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl502 b:35.1 occ:1.00 O A:HOH674 3.1 52.0 1.0 N A:CYS68 3.2 23.2 1.0 N A:VAL67 3.2 26.8 1.0 N A:ALA69 3.2 27.8 1.0 CMD A:HEC501 3.7 25.2 1.0 CB A:ALA69 3.9 34.7 1.0 CA A:ALA66 3.9 37.1 1.0 CA A:CYS68 4.0 24.9 1.0 C2D A:HEC501 4.0 28.8 1.0 C A:VAL67 4.0 27.4 1.0 C A:ALA66 4.0 33.8 1.0 C A:CYS68 4.1 28.0 1.0 CA A:VAL67 4.1 24.7 1.0 CA A:ALA69 4.1 34.4 1.0 C1D A:HEC501 4.3 32.0 1.0 CB A:CYS68 4.3 26.4 1.0 CHD A:HEC501 4.3 27.4 1.0 O A:LYS65 4.5 32.7 1.0 CB A:VAL67 4.6 27.7 1.0 CB A:ALA66 4.6 40.5 1.0 CD A:PRO70 4.7 37.0 1.0 C3D A:HEC501 4.9 28.9 1.0 C4C A:HEC501 4.9 29.7 1.0 CBD A:HEC501 5.0 25.4 1.0

T.Motomura, M.Suga, R.Hienerwadel, A.Nakagawa, T.L.Lai, W.Nitschke, T.Kuma, M.Sugiura, A.Boussac, J.R.Shen. Crystal Structure and Redox Properties of A Novel Cyanobacterial Heme Protein with A His/Cys Heme Axial Ligation and A Per-Arnt-Sim (Pas)-Like Domain J. Biol. Chem. V. 292 9599 2017.
ISSN: ESSN 1083-351X
PubMed: 28428249
DOI: 10.1074/JBC.M116.746263