Magnesium in PDB 5la3: [Fefe]-Hydrogenase Cpi From Clostridium Pasteurianum, Variant E279A

All present enzymatic activity of [Fefe]-Hydrogenase Cpi From Clostridium Pasteurianum, Variant E279A:
1.12.7.2;

The structure of [Fefe]-Hydrogenase Cpi From Clostridium Pasteurianum, Variant E279A, PDB code: 5la3 was solved by J.Duan, J.Esselborn, E.Hofmann, M.Winkler, T.Happe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.46 / 2.29
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	90.480, 73.580, 103.810, 90.00, 96.29, 90.00
R / Rfree (%)	16.6 / 21.3

The structure of [Fefe]-Hydrogenase Cpi From Clostridium Pasteurianum, Variant E279A also contains other interesting chemical elements:

Iron

(Fe)

40 atoms

The binding sites of Magnesium atom in the [Fefe]-Hydrogenase Cpi From Clostridium Pasteurianum, Variant E279A (pdb code 5la3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the [Fefe]-Hydrogenase Cpi From Clostridium Pasteurianum, Variant E279A, PDB code: 5la3:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the [Fefe]-Hydrogenase Cpi From Clostridium Pasteurianum, Variant E279A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of [Fefe]-Hydrogenase Cpi From Clostridium Pasteurianum, Variant E279A within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg607 b:32.6 occ:1.00 O A:HOH755 1.8 31.7 1.0 O A:HOH756 1.9 21.4 1.0 O A:HOH748 2.0 27.0 1.0 O A:HOH795 2.0 28.3 1.0 O A:HOH792 2.0 21.0 1.0 O A:LEU218 2.1 29.7 1.0 C A:LEU218 3.2 27.3 1.0 CA A:LEU218 3.9 24.5 1.0 O A:ALA220 3.9 33.8 1.0 O A:HOH784 4.0 22.7 1.0 N A:ASN219 4.2 25.1 1.0 OD2 A:ASP263 4.4 26.7 1.0 O A:ALA217 4.4 25.1 1.0 OD1 A:ASP263 4.4 33.4 1.0 O A:LYS223 4.4 23.5 1.0 CA A:ASN219 4.5 26.7 1.0 O A:HOH805 4.5 59.8 1.0 C A:ASN219 4.6 27.8 1.0 C A:ALA220 4.7 31.5 1.0 CB A:LEU218 4.8 17.5 1.0 O A:GLY261 4.8 34.9 1.0 CG A:ASP263 4.8 31.7 1.0 N A:ALA220 4.8 26.6 1.0

Magnesium binding site 2 out of 2 in the [Fefe]-Hydrogenase Cpi From Clostridium Pasteurianum, Variant E279A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of [Fefe]-Hydrogenase Cpi From Clostridium Pasteurianum, Variant E279A within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg607 b:30.8 occ:1.00 O B:HOH729 1.9 17.5 1.0 O B:HOH802 2.0 23.4 1.0 O B:HOH748 2.0 27.6 1.0 O B:LEU218 2.1 30.8 1.0 O B:HOH988 2.1 36.4 1.0 O B:HOH791 2.2 20.7 1.0 C B:LEU218 3.3 30.9 1.0 CA B:LEU218 4.0 30.9 1.0 O B:ALA220 4.1 30.8 1.0 O B:HOH775 4.3 25.7 1.0 N B:ASN219 4.3 31.5 1.0 OD2 B:ASP263 4.5 23.8 1.0 OD1 B:ASP263 4.5 27.6 1.0 O B:ALA217 4.6 26.1 1.0 CA B:ASN219 4.6 27.9 1.0 O B:GLY261 4.6 22.9 1.0 O B:LYS223 4.7 24.4 1.0 CB B:LEU218 4.7 24.6 1.0 C B:ASN219 4.8 29.9 1.0 C B:ALA220 4.9 31.8 1.0 N B:ALA220 4.9 28.7 1.0 CG B:ASP263 5.0 26.6 1.0

M.Winkler, M.Senger, J.Duan, J.Esselborn, F.Wittkamp, E.Hofmann, U.P.Apfel, S.T.Stripp, T.Happe. Accumulating the Hydride State in the Catalytic Cycle of [Fefe]-Hydrogenases. Nat Commun V. 8 16115 2017.
ISSN: ESSN 2041-1723
PubMed: 28722011
DOI: 10.1038/NCOMMS16115