Chlorine in PDB 8aio: Co-Bound [Fefe]-Hydrogenase I From Clostridium Pasteurianum (Cpi)

All present enzymatic activity of Co-Bound [Fefe]-Hydrogenase I From Clostridium Pasteurianum (Cpi):
1.12.7.2;

The structure of Co-Bound [Fefe]-Hydrogenase I From Clostridium Pasteurianum (Cpi), PDB code: 8aio was solved by J.Duan, E.Hofmann, T.Happe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.03 / 1.52
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	87.6, 72.16, 103.21, 90, 101.94, 90
R / Rfree (%)	16.7 / 19.2

The structure of Co-Bound [Fefe]-Hydrogenase I From Clostridium Pasteurianum (Cpi) also contains other interesting chemical elements:

Magnesium	(Mg)	4 atoms
Iron	(Fe)	40 atoms

The binding sites of Chlorine atom in the Co-Bound [Fefe]-Hydrogenase I From Clostridium Pasteurianum (Cpi) (pdb code 8aio). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Co-Bound [Fefe]-Hydrogenase I From Clostridium Pasteurianum (Cpi), PDB code: 8aio:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Co-Bound [Fefe]-Hydrogenase I From Clostridium Pasteurianum (Cpi)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Co-Bound [Fefe]-Hydrogenase I From Clostridium Pasteurianum (Cpi) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl610 b:31.6 occ:1.00 H A:ALA406 2.6 27.0 1.0 HD2 A:PRO405 2.6 35.3 1.0 HB3 A:ASP404 2.6 31.3 1.0 O A:HOH1033 3.0 37.7 1.0 HB1 A:ALA406 3.1 31.1 1.0 HB2 A:ALA406 3.1 31.1 1.0 HE1 A:PHE266 3.2 22.7 1.0 HE3 A:LYS264 3.2 45.8 1.0 CD A:PRO405 3.4 29.4 1.0 N A:ALA406 3.4 22.5 1.0 CB A:ALA406 3.5 26.0 1.0 CB A:ASP404 3.5 26.1 1.0 HZ2 A:LYS264 3.6 49.3 1.0 N A:PRO405 3.6 25.8 1.0 HG2 A:PRO405 3.7 38.8 1.0 C A:ASP404 3.8 28.0 1.0 CE A:LYS264 3.9 38.2 1.0 HE2 A:LYS264 3.9 45.8 1.0 HB2 A:ASP404 3.9 31.3 1.0 HA A:ASP404 4.0 30.4 1.0 CE1 A:PHE266 4.0 18.9 1.0 CA A:ASP404 4.0 25.4 1.0 HZ A:PHE266 4.0 27.2 1.0 CA A:ALA406 4.1 23.3 1.0 CG A:PRO405 4.1 32.3 1.0 NZ A:LYS264 4.1 41.1 1.0 HD3 A:PRO405 4.1 35.3 1.0 O A:HOH1037 4.2 48.6 1.0 HB3 A:ALA406 4.4 31.1 1.0 HZ3 A:LYS264 4.4 49.3 1.0 C A:PRO405 4.4 25.0 1.0 O A:ASP404 4.5 24.3 1.0 CZ A:PHE266 4.5 22.7 1.0 CA A:PRO405 4.5 28.2 1.0 CG A:ASP404 4.5 34.5 1.0 H A:MET407 4.6 27.0 1.0 HA A:ALA406 4.7 28.0 1.0 OD1 A:ASP404 4.8 34.4 1.0 HG3 A:PRO405 4.8 38.8 1.0 HZ1 A:LYS264 4.9 49.3 1.0

Chlorine binding site 2 out of 2 in the Co-Bound [Fefe]-Hydrogenase I From Clostridium Pasteurianum (Cpi)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Co-Bound [Fefe]-Hydrogenase I From Clostridium Pasteurianum (Cpi) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl610 b:27.9 occ:1.00 H B:ALA406 2.5 23.9 1.0 HB3 B:ASP404 2.7 27.2 1.0 HD2 B:PRO405 2.7 36.4 1.0 O B:HOH1030 3.0 35.8 1.0 O B:HOH1086 3.1 44.4 1.0 HB2 B:ALA406 3.1 28.4 1.0 HE1 B:PHE266 3.2 23.9 1.0 HB3 B:ALA406 3.2 28.4 1.0 HE3 B:LYS264 3.2 47.1 1.0 N B:ALA406 3.4 19.9 1.0 CD B:PRO405 3.5 30.4 1.0 CB B:ALA406 3.5 23.7 1.0 N B:PRO405 3.6 23.0 1.0 CB B:ASP404 3.6 22.7 1.0 HZ1 B:LYS264 3.6 51.6 1.0 HG2 B:PRO405 3.7 36.3 1.0 C B:ASP404 3.8 23.9 1.0 HE2 B:LYS264 3.8 47.1 1.0 CE B:LYS264 3.9 39.3 1.0 HA B:ASP404 3.9 23.9 1.0 CE1 B:PHE266 4.0 19.9 1.0 HB2 B:ASP404 4.0 27.2 1.0 CA B:ASP404 4.0 19.9 1.0 HZ B:PHE266 4.0 23.6 1.0 CA B:ALA406 4.1 22.9 1.0 CG B:PRO405 4.1 30.2 1.0 NZ B:LYS264 4.2 43.0 1.0 HD3 B:PRO405 4.2 36.4 1.0 C B:PRO405 4.4 22.1 1.0 HB1 B:ALA406 4.4 28.4 1.0 O B:ASP404 4.4 21.9 1.0 CZ B:PHE266 4.4 19.7 1.0 CA B:PRO405 4.5 24.2 1.0 HZ2 B:LYS264 4.6 51.6 1.0 CG B:ASP404 4.6 31.2 1.0 H B:MET407 4.6 23.8 1.0 HA B:ALA406 4.7 27.5 1.0 OD1 B:ASP404 4.8 28.9 1.0 HG3 B:PRO405 4.8 36.3 1.0 HZ3 B:LYS264 4.9 51.6 1.0 CB B:PRO405 5.0 30.6 1.0

J.Duan, A.Hemschemeier, D.J.Burr, S.T.Stripp, E.Hofmann, T.Happe. Cyanide Binding to [Fefe]-Hydrogenase Stabilizes the Alternative Configuration of the Proton Transfer Pathway. Angew.Chem.Int.Ed.Engl. 2022.
ISSN: ESSN 1521-3773
PubMed: 36464641
DOI: 10.1002/ANIE.202216903