Iron in PDB 6ggu: Crystal Structure of Native Fe-Hydrogenase From Methanothermobacter Marburgensis

All present enzymatic activity of Crystal Structure of Native Fe-Hydrogenase From Methanothermobacter Marburgensis:
1.12.98.2;

The structure of Crystal Structure of Native Fe-Hydrogenase From Methanothermobacter Marburgensis, PDB code: 6ggu was solved by T.Wagner, G.Huang, U.Ermler, S.Shima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.84 / 2.60
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	144.060, 144.060, 95.060, 90.00, 90.00, 120.00
R / Rfree (%)	18.8 / 23.5

The binding sites of Iron atom in the Crystal Structure of Native Fe-Hydrogenase From Methanothermobacter Marburgensis (pdb code 6ggu). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystal Structure of Native Fe-Hydrogenase From Methanothermobacter Marburgensis, PDB code: 6ggu:

Iron binding site 1 out of 1 in the Crystal Structure of Native Fe-Hydrogenase From Methanothermobacter Marburgensis


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 From Methanothermobacter Marburgensis within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe405 b:29.5 occ:1.00 FE A:FE9405 0.0 29.5 1.0 C2F A:FE9405 1.8 30.4 1.0 C1F A:FE9405 1.8 34.1 1.0 C8 A:FE9405 1.9 30.2 1.0 N1 A:FE9405 1.9 24.9 1.0 SG A:CYS172 2.6 25.6 1.0 O18 A:FE9405 2.7 31.0 1.0 C6 A:FE9405 2.8 25.2 1.0 C2 A:FE9405 2.9 23.5 1.0 O2F A:FE9405 2.9 34.9 1.0 C7 A:FE9405 2.9 27.6 1.0 O1F A:FE9405 3.0 31.3 1.0 O2 A:FE9405 3.1 28.7 1.0 CB A:CYS172 3.6 21.3 1.0 C5 A:FE9405 4.3 25.2 1.0 C3 A:FE9405 4.3 25.4 1.0 CH2 A:TRP144 4.3 25.0 1.0 CZ2 A:TRP144 4.5 25.8 1.0 CA A:CYS172 4.8 21.2 1.0 C4 A:FE9405 4.8 27.7 1.0 N A:CYS172 4.8 21.6 1.0 O A:ALA206 4.9 21.0 1.0 CG A:PRO204 5.0 21.8 1.0

T.Wagner, G.Huang, U.Ermler, S.Shima. Self-Protection of the Catalytic Iron Center of A Methanogenic [Fe]-Hydrogenase Via A Dynamic Dimer-to-Hexamer Transformation To Be Published.