Chlorine in PDB 5giz: Periplasmic Heme-Binding Protein Bhut in Apo Form

The structure of Periplasmic Heme-Binding Protein Bhut in Apo Form, PDB code: 5giz was solved by N.Nakamura, Y.Naoe, M.M.Rahman, Y.Shiro, H.Sugimoto, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.45 / 1.50
Space group	P 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	45.983, 46.443, 222.292, 90.00, 90.00, 90.00
R / Rfree (%)	17.4 / 21.2

The binding sites of Chlorine atom in the Periplasmic Heme-Binding Protein Bhut in Apo Form (pdb code 5giz). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Periplasmic Heme-Binding Protein Bhut in Apo Form, PDB code: 5giz:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Periplasmic Heme-Binding Protein Bhut in Apo Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Periplasmic Heme-Binding Protein Bhut in Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl403 b:16.9 occ:1.00 O A:HOH772 3.0 25.9 1.0 NE A:ARG299 3.2 12.9 1.0 NH1 A:ARG298 3.3 15.2 1.0 NH2 A:ARG299 3.4 13.5 1.0 NH2 B:ARG299 3.4 12.8 1.0 CD2 B:LEU277 3.6 14.0 1.0 O A:HOH739 3.7 25.0 1.0 CD A:ARG298 3.7 13.3 1.0 CZ A:ARG299 3.7 13.8 1.0 CD B:ARG299 3.8 12.9 1.0 CG2 A:THR295 3.8 10.5 1.0 CG A:ARG299 4.0 11.6 1.0 CZ B:ARG299 4.1 13.4 1.0 CD A:ARG299 4.2 12.1 1.0 CZ A:ARG298 4.2 15.1 1.0 NE B:ARG299 4.3 13.0 1.0 NE A:ARG298 4.4 13.9 1.0 CG B:ARG299 4.5 12.0 1.0 O B:HOH698 4.6 13.9 1.0 CG2 B:THR295 4.6 10.9 1.0 CG A:ARG298 4.7 12.1 1.0 O B:SER276 4.7 10.5 1.0 O A:THR295 4.9 11.2 1.0 CB A:THR295 4.9 10.5 1.0 CG B:LEU277 5.0 12.3 1.0

Chlorine binding site 2 out of 2 in the Periplasmic Heme-Binding Protein Bhut in Apo Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Periplasmic Heme-Binding Protein Bhut in Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl402 b:25.1 occ:1.00 OD2 B:ASP302 2.7 11.9 1.0 NE B:ARG299 2.8 13.0 1.0 O A:HOH660 2.9 15.3 1.0 O B:HOH653 3.3 12.8 1.0 CD A:ARG299 3.5 12.1 1.0 CG B:ASP302 3.6 12.3 1.0 NH1 B:ARG299 3.6 13.2 1.0 CB B:ASP302 3.6 11.5 1.0 CZ B:ARG299 3.6 13.4 1.0 CD B:ARG299 3.7 12.9 1.0 CG A:ARG299 3.8 11.6 1.0 CB A:ARG299 3.8 10.8 1.0 CG1 A:VAL275 4.2 11.8 1.0 NE A:ARG299 4.2 12.9 1.0 O A:HOH697 4.2 22.0 1.0 NH1 A:ARG299 4.3 15.0 1.0 CG2 A:VAL275 4.4 11.2 1.0 O A:HOH650 4.4 40.6 1.0 CA A:VAL275 4.4 11.0 1.0 CA B:ARG299 4.5 10.6 1.0 CZ A:ARG299 4.6 13.8 1.0 O A:SER276 4.6 12.1 1.0 CB A:VAL275 4.6 11.2 1.0 N A:SER276 4.6 11.4 1.0 CA A:ARG299 4.7 10.5 1.0 OD1 B:ASP302 4.8 13.2 1.0 O B:ARG299 4.8 10.5 1.0 O A:VAL274 4.8 11.6 1.0 NH2 B:ARG299 4.8 12.8 1.0 CG B:ARG299 4.9 12.0 1.0 CB B:ARG299 4.9 11.1 1.0 O A:ARG299 5.0 10.5 1.0

Y.Naoe, N.Nakamura, M.M.Rahman, T.Tosha, S.Nagatoishi, K.Tsumoto, Y.Shiro, H.Sugimoto. Structural Basis For Binding and Transfer of Heme in Bacterial Heme-Acquisition Systems. Proteins V. 85 2217 2017.
ISSN: ESSN 1097-0134
PubMed: 28913898
DOI: 10.1002/PROT.25386