Magnesium in PDB 6ehq: E. Coli Hydrogenase-2 (As Isolated Form).

All present enzymatic activity of E. Coli Hydrogenase-2 (As Isolated Form).:
1.12.99.6;

The structure of E. Coli Hydrogenase-2 (As Isolated Form)., PDB code: 6ehq was solved by S.B.Carr, S.E.Beaton, R.M.Evans, F.A.Armstrong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	86.00 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	99.064, 100.090, 168.135, 90.00, 90.00, 90.00
R / Rfree (%)	16.2 / 19

The structure of E. Coli Hydrogenase-2 (As Isolated Form). also contains other interesting chemical elements:

Nickel	(Ni)	2 atoms
Iron	(Fe)	26 atoms

The binding sites of Magnesium atom in the E. Coli Hydrogenase-2 (As Isolated Form). (pdb code 6ehq). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the E. Coli Hydrogenase-2 (As Isolated Form)., PDB code: 6ehq:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the E. Coli Hydrogenase-2 (As Isolated Form).


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of E. Coli Hydrogenase-2 (As Isolated Form). within 5.0Å range: probe atom residue distance (Å) B Occ L:Mg603 b:14.1 occ:1.00 OE2 L:GLU42 2.0 22.7 1.0 O L:HOH740 2.0 18.8 1.0 O L:HOH713 2.0 22.2 1.0 O L:HOH710 2.0 13.7 1.0 O L:ALA498 2.1 20.3 1.0 NE2 L:HIS552 2.2 22.7 1.0 CD L:GLU42 3.0 23.1 1.0 CD2 L:HIS552 3.2 22.4 1.0 CE1 L:HIS552 3.2 22.9 1.0 C L:ALA498 3.3 22.2 1.0 OE1 L:GLU42 3.3 23.5 1.0 N L:ALA498 3.7 21.6 1.0 OE1 L:GLN497 3.9 28.6 1.0 CA L:ALA498 3.9 21.7 1.0 OE1 L:GLU329 4.1 28.5 1.0 OE2 L:GLU329 4.1 28.1 1.0 O L:HOH768 4.2 20.9 1.0 CG L:GLU42 4.3 22.9 1.0 O L:HOH805 4.3 19.6 1.0 CB L:ALA498 4.3 21.8 1.0 ND1 L:HIS552 4.3 22.2 1.0 CG L:HIS552 4.3 21.8 1.0 NZ L:LYS366 4.3 22.7 1.0 N L:VAL499 4.4 21.4 1.0 CD L:GLU329 4.6 28.7 1.0 C L:GLN497 4.6 23.0 1.0 CD L:LYS366 4.7 21.9 1.0 CA L:VAL499 4.8 22.0 1.0 CA L:GLN497 4.9 23.5 1.0 CD L:GLN497 4.9 26.1 1.0 CE L:LYS366 5.0 22.0 1.0

Magnesium binding site 2 out of 2 in the E. Coli Hydrogenase-2 (As Isolated Form).


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of E. Coli Hydrogenase-2 (As Isolated Form). within 5.0Å range: probe atom residue distance (Å) B Occ M:Mg603 b:19.8 occ:1.00 O M:HOH743 2.0 22.1 1.0 O M:HOH706 2.0 21.6 1.0 OE2 M:GLU42 2.1 23.2 1.0 O M:HOH710 2.1 20.9 1.0 O M:ALA498 2.1 23.5 1.0 NE2 M:HIS552 2.1 24.0 1.0 CD M:GLU42 3.1 24.9 1.0 CE1 M:HIS552 3.1 24.9 1.0 CD2 M:HIS552 3.1 23.9 1.0 C M:ALA498 3.3 23.1 1.0 OE1 M:GLU42 3.4 24.8 1.0 N M:ALA498 3.7 23.0 1.0 CA M:ALA498 4.0 23.4 1.0 OE1 M:GLN497 4.0 26.4 1.0 O M:HOH718 4.1 19.5 1.0 OE2 M:GLU329 4.2 36.9 1.0 ND1 M:HIS552 4.2 23.8 1.0 CG M:HIS552 4.2 23.9 1.0 OE1 M:GLU329 4.3 34.9 1.0 O M:HOH771 4.3 25.2 1.0 CB M:ALA498 4.3 23.1 1.0 CG M:GLU42 4.4 25.3 1.0 N M:VAL499 4.4 23.1 1.0 NZ M:LYS366 4.4 27.7 1.0 CD M:LYS366 4.6 26.4 1.0 CD M:GLU329 4.6 34.8 1.0 C M:GLN497 4.7 23.2 1.0 CA M:VAL499 4.8 23.9 1.0 CE M:LYS366 4.9 27.0 1.0 CA M:GLN497 5.0 24.0 1.0

S.E.Beaton, R.M.Evans, A.J.Finney, C.M.Lamont, F.A.Armstrong, F.Sargent, S.B.Carr. The Structure of Hydrogenase-2 Fromescherichia Coli: Implications For H2-Driven Proton Pumping. Biochem. J. V. 475 1353 2018.
ISSN: ESSN 1470-8728
PubMed: 29555844
DOI: 10.1042/BCJ20180053