Magnesium in PDB 8dqv: The 1.52 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L)

All present enzymatic activity of The 1.52 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L):
1.12.99.6;

The structure of The 1.52 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L) also contains other interesting chemical elements:

Iron	(Fe)	20 atoms
Nickel	(Ni)	2 atoms

The binding sites of Magnesium atom in the The 1.52 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L) (pdb code 8dqv). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the The 1.52 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L), PDB code: 8dqv:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the The 1.52 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The 1.52 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg602 b:7.5 occ:1.00 O A:VAL462 1.9 5.4 1.0 O A:HOH706 2.1 6.6 1.0 OE2 A:GLU43 2.1 6.2 1.0 NE2 A:HIS516 2.1 5.5 1.0 O A:HOH758 2.1 6.5 1.0 O A:HOH740 2.2 8.2 1.0 CD A:GLU43 3.0 6.2 1.0 H A:VAL462 3.0 5.4 1.0 CE1 A:HIS516 3.0 5.5 1.0 C A:VAL462 3.1 5.4 1.0 CD2 A:HIS516 3.1 5.5 1.0 HE1 A:HIS516 3.2 5.5 1.0 OE1 A:GLU43 3.3 6.2 1.0 HD2 A:HIS516 3.3 5.5 1.0 HZ2 A:LYS341 3.4 7.6 1.0 N A:VAL462 3.6 5.4 1.0 HB A:VAL462 3.7 5.4 1.0 HA A:VAL463 3.8 5.8 1.0 OE2 A:GLU303 3.8 8.3 1.0 HD2 A:LYS341 3.8 7.6 1.0 CA A:VAL462 3.8 5.4 1.0 OE1 A:GLU303 3.9 8.3 1.0 OE1 A:GLN461 3.9 6.4 1.0 N A:VAL463 4.1 5.8 1.0 ND1 A:HIS516 4.1 5.5 1.0 O A:HOH733 4.2 6.4 1.0 HG22 A:VAL463 4.2 5.8 1.0 CG A:HIS516 4.2 5.5 1.0 O A:HOH736 4.2 6.9 1.0 NZ A:LYS341 4.2 7.6 1.0 CD A:GLU303 4.3 8.3 1.0 CB A:VAL462 4.3 5.4 1.0 CG A:GLU43 4.3 6.2 1.0 HA A:GLN461 4.4 6.4 1.0 HG3 A:LYS341 4.4 7.6 1.0 CA A:VAL463 4.4 5.8 1.0 HG3 A:GLU43 4.5 6.2 1.0 HE3 A:LYS341 4.5 7.6 1.0 HG2 A:GLU43 4.5 6.2 1.0 CD A:LYS341 4.6 7.6 1.0 HB3 A:GLN461 4.6 6.4 1.0 C A:GLN461 4.6 6.4 1.0 HZ3 A:LYS341 4.7 7.6 1.0 HG1 A:THR323 4.7 7.6 1.0 CE A:LYS341 4.7 7.6 1.0 HZ1 A:LYS341 4.7 7.6 1.0 HA A:VAL462 4.7 5.4 1.0 HG23 A:VAL463 4.8 5.8 1.0 CG2 A:VAL463 4.9 5.8 1.0 H A:VAL463 4.9 5.8 1.0 HD1 A:HIS516 4.9 5.5 1.0 HB2 A:LYS341 4.9 7.6 1.0 CA A:GLN461 4.9 6.4 1.0 HG23 A:VAL462 5.0 5.4 1.0 HG12 A:VAL462 5.0 5.4 1.0 O A:VAL515 5.0 6.2 1.0 CG A:LYS341 5.0 7.6 1.0

Magnesium binding site 2 out of 2 in the The 1.52 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of The 1.52 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L) within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg602 b:7.5 occ:1.00 O C:VAL462 1.9 5.4 1.0 O C:HOH707 2.1 6.6 1.0 NE2 C:HIS516 2.1 5.5 1.0 OE2 C:GLU43 2.1 6.2 1.0 O C:HOH759 2.1 6.5 1.0 O C:HOH740 2.2 8.2 1.0 CD C:GLU43 3.0 6.2 1.0 H C:VAL462 3.0 5.4 1.0 CE1 C:HIS516 3.0 5.5 1.0 C C:VAL462 3.1 5.4 1.0 CD2 C:HIS516 3.1 5.5 1.0 HE1 C:HIS516 3.2 5.5 1.0 OE1 C:GLU43 3.3 6.2 1.0 HD2 C:HIS516 3.3 5.5 1.0 HZ2 C:LYS341 3.4 7.6 1.0 N C:VAL462 3.6 5.4 1.0 HB C:VAL462 3.6 5.4 1.0 HA C:VAL463 3.8 5.9 1.0 OE2 C:GLU303 3.8 8.3 1.0 HD2 C:LYS341 3.8 7.6 1.0 CA C:VAL462 3.8 5.4 1.0 OE1 C:GLU303 3.9 8.3 1.0 OE1 C:GLN461 3.9 6.4 1.0 N C:VAL463 4.1 5.9 1.0 ND1 C:HIS516 4.1 5.5 1.0 O C:HOH733 4.2 6.4 1.0 HG22 C:VAL463 4.2 5.9 1.0 CG C:HIS516 4.2 5.5 1.0 O C:HOH736 4.2 6.9 1.0 NZ C:LYS341 4.2 7.6 1.0 CD C:GLU303 4.3 8.3 1.0 CB C:VAL462 4.3 5.4 1.0 CG C:GLU43 4.3 6.2 1.0 HA C:GLN461 4.4 6.4 1.0 HG3 C:LYS341 4.4 7.6 1.0 CA C:VAL463 4.4 5.9 1.0 HG3 C:GLU43 4.5 6.2 1.0 HE3 C:LYS341 4.5 7.6 1.0 HG2 C:GLU43 4.5 6.2 1.0 CD C:LYS341 4.6 7.6 1.0 HB3 C:GLN461 4.6 6.4 1.0 C C:GLN461 4.6 6.4 1.0 HZ3 C:LYS341 4.7 7.6 1.0 HG1 C:THR323 4.7 7.7 1.0 CE C:LYS341 4.7 7.6 1.0 HZ1 C:LYS341 4.7 7.6 1.0 HA C:VAL462 4.7 5.4 1.0 HG23 C:VAL463 4.8 5.9 1.0 CG2 C:VAL463 4.9 5.9 1.0 H C:VAL463 4.9 5.9 1.0 HD1 C:HIS516 4.9 5.5 1.0 HB2 C:LYS341 4.9 7.6 1.0 CA C:GLN461 4.9 6.4 1.0 HG23 C:VAL462 5.0 5.4 1.0 HG12 C:VAL462 5.0 5.4 1.0 O C:VAL515 5.0 6.2 1.0 CG C:LYS341 5.0 7.6 1.0

R.Grinter, A.Kropp, H.Venugopal, M.Senger, J.Badley, P.Cabotaje, S.T.Stripp, C.K.Barlow, M.Belousoff, G.M.Cook, R.B.Schittenhelm, S.Khalid, G.Berggren, G.Greening. Energy Extraction From Air: Structural Basis of Atmospheric Hydrogen Oxidation To Be Published.