Iron in PDB 5ok4: Crystal Structure of Native [Fe]-Hydrogenase Hmd From Methanothermobacter Marburgensis Inactivated By O2.

All present enzymatic activity of Crystal Structure of Native [Fe]-Hydrogenase Hmd From Methanothermobacter Marburgensis Inactivated By O2.:
1.12.98.2;

The structure of Crystal Structure of Native [Fe]-Hydrogenase Hmd From Methanothermobacter Marburgensis Inactivated By O2., PDB code: 5ok4 was solved by T.Wagner, G.Huang, E.Bill, U.Ermler, K.Ataka, S.Shima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.47 / 1.29
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	127.418, 127.418, 141.211, 90.00, 90.00, 120.00
R / Rfree (%)	12.7 / 14.7

The binding sites of Iron atom in the Crystal Structure of Native [Fe]-Hydrogenase Hmd From Methanothermobacter Marburgensis Inactivated By O2. (pdb code 5ok4). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Crystal Structure of Native [Fe]-Hydrogenase Hmd From Methanothermobacter Marburgensis Inactivated By O2., PDB code: 5ok4:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the Crystal Structure of Native [Fe]-Hydrogenase Hmd From Methanothermobacter Marburgensis Inactivated By O2.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Native [Fe]-Hydrogenase Hmd From Methanothermobacter Marburgensis Inactivated By O2. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:12.4 occ:1.00 O28 A:FEG404 2.0 14.4 1.0 NE2 A:HIS203 2.0 14.2 1.0 SG A:CYS172 2.3 14.5 1.0 C8 A:FEG404 2.7 13.9 1.0 O18 A:FEG404 2.8 14.7 1.0 CE1 A:HIS203 2.9 15.2 1.0 CD2 A:HIS203 3.0 15.0 1.0 CB A:CYS172 3.2 13.6 1.0 O A:HOH597 3.9 21.1 1.0 ND1 A:HIS203 4.1 15.1 1.0 C7 A:FEG404 4.1 13.8 1.0 CG A:HIS203 4.2 14.8 1.0 N A:CYS172 4.2 14.0 1.0 CA A:CYS172 4.3 13.6 1.0 N1 A:FEG404 4.5 13.8 1.0 C6 A:FEG404 4.7 13.5 1.0 O A:PRO204 4.8 18.7 1.0 O A:HOH917 4.8 49.8 1.0 CH2 A:TRP144 4.9 17.5 1.0

Iron binding site 2 out of 3 in the Crystal Structure of Native [Fe]-Hydrogenase Hmd From Methanothermobacter Marburgensis Inactivated By O2.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Native [Fe]-Hydrogenase Hmd From Methanothermobacter Marburgensis Inactivated By O2. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe402 b:13.5 occ:1.00 O A:GLY249 2.1 14.8 1.0 SG A:CYS252 2.2 14.5 1.0 SG A:CYS255 2.3 15.6 1.0 C A:GLY249 3.1 14.0 1.0 CB A:CYS255 3.1 15.2 1.0 CB A:CYS252 3.3 15.0 1.0 CA A:GLY249 3.7 15.0 1.0 N A:CYS255 4.0 14.2 1.0 N A:CYS252 4.1 14.6 1.0 N A:PRO250 4.1 13.8 1.0 CA A:CYS252 4.2 14.5 1.0 CA A:CYS255 4.2 15.0 1.0 CA A:PRO250 4.4 14.4 1.0 CB A:MET254 4.7 18.3 1.0 C A:CYS252 4.7 14.2 1.0 C A:PRO250 4.7 14.0 1.0 O A:CYS252 4.8 14.3 1.0 C A:MET254 4.8 15.3 1.0 O A:HOH912 4.8 17.8 1.0 O A:LEU248 5.0 17.5 1.0 N A:VAL251 5.0 14.1 1.0 N A:MET254 5.0 15.0 1.0

Iron binding site 3 out of 3 in the Crystal Structure of Native [Fe]-Hydrogenase Hmd From Methanothermobacter Marburgensis Inactivated By O2.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of Native [Fe]-Hydrogenase Hmd From Methanothermobacter Marburgensis Inactivated By O2. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe403 b:13.6 occ:0.33 OD2 A:ASP153 2.0 15.6 1.0 O A:HOH871 2.0 24.5 0.3 CG A:ASP153 2.8 15.5 1.0 OD1 A:ASP153 2.9 16.9 1.0 O A:HOH566 4.0 47.5 1.0 CB A:ASP153 4.2 14.8 1.0 O A:HOH726 4.2 20.3 1.0

G.Huang, T.Wagner, U.Ermler, E.Bill, K.Ataka, S.Shima. Dioxygen Sensitivity of [Fe]-Hydrogenase in the Presence of Reducing Substrates. Angew. Chem. Int. Ed. Engl. V. 57 4917 2018.
ISSN: ESSN 1521-3773
PubMed: 29462510
DOI: 10.1002/ANIE.201712293