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Chlorine in PDB 8aln: Co-Bound [Fefe]-Hydrogenase I From Clostridium Pasteurianum (Cpi) at 1.34 Angstrom

Enzymatic activity of Co-Bound [Fefe]-Hydrogenase I From Clostridium Pasteurianum (Cpi) at 1.34 Angstrom

All present enzymatic activity of Co-Bound [Fefe]-Hydrogenase I From Clostridium Pasteurianum (Cpi) at 1.34 Angstrom:
1.12.7.2;

Protein crystallography data

The structure of Co-Bound [Fefe]-Hydrogenase I From Clostridium Pasteurianum (Cpi) at 1.34 Angstrom, PDB code: 8aln 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) 47.10 / 1.34
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 89.86, 71.85, 103.23, 90, 97.47, 90
R / Rfree (%) 14.9 / 17.5

Other elements in 8aln:

The structure of Co-Bound [Fefe]-Hydrogenase I From Clostridium Pasteurianum (Cpi) at 1.34 Angstrom also contains other interesting chemical elements:

Iron (Fe) 40 atoms
Magnesium (Mg) 6 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Co-Bound [Fefe]-Hydrogenase I From Clostridium Pasteurianum (Cpi) at 1.34 Angstrom (pdb code 8aln). 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 Co-Bound [Fefe]-Hydrogenase I From Clostridium Pasteurianum (Cpi) at 1.34 Angstrom, PDB code: 8aln:

Chlorine binding site 1 out of 1 in 8aln

Go back to Chlorine Binding Sites List in 8aln
Chlorine binding site 1 out of 1 in the Co-Bound [Fefe]-Hydrogenase I From Clostridium Pasteurianum (Cpi) at 1.34 Angstrom


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) at 1.34 Angstrom within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl612

b:30.2
occ:1.00
 O B:HOH1202 2.8 37.1 1.0
O B:HOH1119 3.0 49.9 1.0
O B:HOH1208 3.0 42.2 1.0
N B:ALA406 3.3 23.1 1.0
CB B:ALA406 3.5 22.0 1.0
CD B:PRO405 3.6 24.7 1.0
N B:PRO405 3.6 23.6 1.0
CB B:ASP404 3.6 23.8 1.0
CE B:LYS264 3.8 33.4 1.0
C B:ASP404 3.9 22.9 1.0
CE1 B:PHE266 4.0 20.0 1.0
CA B:ALA406 4.0 22.2 1.0
CG B:PRO405 4.1 26.7 1.0
CA B:ASP404 4.1 23.6 1.0
NZ B:LYS264 4.2 35.1 1.0
O B:HOH1258 4.2 42.7 1.0
C B:PRO405 4.3 24.0 1.0
CZ B:PHE266 4.4 20.3 1.0
CA B:PRO405 4.5 24.6 1.0
O B:ASP404 4.5 23.4 1.0
CG B:ASP404 4.7 26.5 1.0
CB B:PRO405 4.9 25.8 1.0
OD1 B:ASP404 4.9 29.6 1.0

Reference:

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
Page generated: Sun Jul 13 09:10:41 2025

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