Nickel 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
Magnesium	(Mg)	2 atoms

The binding sites of Nickel 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 Nickel atom.
In total 2 binding sites of Nickel 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 Nickel binding site number: 1; 2;

Nickel 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 Nickel with other atoms in the Ni 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:Ni604 b:42.8 occ:1.00 O A:O601 1.7 20.0 1.0 SG A:CYS62 2.4 4.5 1.0 SG A:CYS510 2.4 6.6 1.0 SG A:CYS513 2.5 5.6 1.0 SG A:CYS65 2.6 5.1 1.0 FE A:FCO603 2.6 7.4 1.0 HB2 A:CYS62 3.0 4.5 1.0 HG22 A:ILE64 3.1 5.4 1.0 CB A:CYS62 3.1 4.5 1.0 CB A:CYS510 3.1 6.6 1.0 HB3 A:CYS510 3.1 6.6 1.0 HB2 A:CYS510 3.1 6.6 1.0 HB3 A:CYS62 3.2 4.5 1.0 HB3 A:CYS65 3.3 5.1 1.0 HB2 A:CYS513 3.4 5.6 1.0 HG23 A:ILE64 3.6 5.4 1.0 CB A:CYS65 3.6 5.1 1.0 CB A:CYS513 3.6 5.6 1.0 H A:CYS65 3.6 5.1 1.0 C1 A:FCO603 3.6 7.4 1.0 HD2 A:ARG443 3.7 6.8 1.0 CG2 A:ILE64 3.7 5.4 1.0 C2 A:FCO603 3.7 7.4 1.0 HG23 A:VAL512 3.8 5.7 1.0 H A:CYS513 3.9 5.6 1.0 HG21 A:ILE64 4.0 5.4 1.0 N A:CYS65 4.1 5.1 1.0 HH11 A:ARG443 4.3 6.8 1.0 C3 A:FCO603 4.3 7.4 1.0 HG22 A:VAL512 4.3 5.7 1.0 HB3 A:CYS513 4.3 5.6 1.0 H A:ILE64 4.3 5.4 1.0 CD A:ARG443 4.4 6.8 1.0 HB2 A:CYS65 4.4 5.1 1.0 HD3 A:ARG443 4.4 6.8 1.0 CA A:CYS65 4.4 5.1 1.0 CG2 A:VAL512 4.4 5.7 1.0 N A:CYS513 4.4 5.6 1.0 CA A:CYS62 4.5 4.5 1.0 HE2 A:HIS69 4.5 4.5 1.0 N1 A:FCO603 4.5 7.4 1.0 CA A:CYS513 4.5 5.6 1.0 CA A:CYS510 4.5 6.6 1.0 NH1 A:ARG443 4.6 6.8 1.0 N2 A:FCO603 4.6 7.4 1.0 HA A:CYS62 4.6 4.5 1.0 HB3 A:GLU15 4.6 7.1 1.0 HA A:CYS513 4.7 5.6 1.0 NE A:ARG443 4.7 6.8 1.0 HG21 A:VAL512 4.7 5.7 1.0 HG3 A:GLU15 4.8 7.1 1.0 HA A:CYS510 4.8 6.6 1.0 CZ A:ARG443 4.8 6.8 1.0 HB2 A:GLU15 4.9 7.1 1.0 HH12 A:ARG443 5.0 6.8 1.0 C A:CYS62 5.0 4.5 1.0

Nickel 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 Nickel with other atoms in the Ni 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:Ni604 b:42.5 occ:1.00 O C:O601 1.7 20.0 1.0 SG C:CYS62 2.4 4.4 1.0 SG C:CYS510 2.4 6.6 1.0 SG C:CYS513 2.5 5.7 1.0 SG C:CYS65 2.5 5.1 1.0 FE C:FCO603 2.6 7.4 1.0 HB2 C:CYS62 3.0 4.4 1.0 CB C:CYS62 3.1 4.4 1.0 CB C:CYS510 3.1 6.6 1.0 HB3 C:CYS510 3.1 6.6 1.0 HB2 C:CYS510 3.1 6.6 1.0 HB3 C:CYS62 3.2 4.4 1.0 HG22 C:ILE64 3.2 5.4 1.0 HG23 C:ILE64 3.3 5.4 1.0 HB3 C:CYS65 3.3 5.1 1.0 HB2 C:CYS513 3.4 5.7 1.0 CB C:CYS65 3.6 5.1 1.0 CB C:CYS513 3.6 5.7 1.0 H C:CYS65 3.6 5.1 1.0 C1 C:FCO603 3.6 7.4 1.0 HD2 C:ARG443 3.7 6.8 1.0 CG2 C:ILE64 3.7 5.4 1.0 C2 C:FCO603 3.7 7.4 1.0 HG23 C:VAL512 3.8 5.7 1.0 H C:CYS513 3.9 5.7 1.0 HG21 C:ILE64 4.0 5.4 1.0 N C:CYS65 4.1 5.1 1.0 HH11 C:ARG443 4.3 6.8 1.0 HB3 C:CYS513 4.3 5.7 1.0 C3 C:FCO603 4.3 7.4 1.0 H C:ILE64 4.3 5.4 1.0 HG22 C:VAL512 4.4 5.7 1.0 CD C:ARG443 4.4 6.8 1.0 HB2 C:CYS65 4.4 5.1 1.0 HD3 C:ARG443 4.4 6.8 1.0 CA C:CYS65 4.4 5.1 1.0 CG2 C:VAL512 4.4 5.7 1.0 N C:CYS513 4.5 5.7 1.0 CA C:CYS62 4.5 4.4 1.0 N1 C:FCO603 4.5 7.4 1.0 HE2 C:HIS69 4.5 4.4 1.0 CA C:CYS513 4.5 5.7 1.0 CA C:CYS510 4.5 6.6 1.0 NH1 C:ARG443 4.6 6.8 1.0 N2 C:FCO603 4.6 7.4 1.0 HA C:CYS62 4.6 4.4 1.0 HB3 C:GLU15 4.6 7.1 1.0 HG21 C:VAL512 4.7 5.7 1.0 HA C:CYS513 4.7 5.7 1.0 NE C:ARG443 4.7 6.8 1.0 HG3 C:GLU15 4.8 7.1 1.0 HA C:CYS510 4.8 6.6 1.0 CZ C:ARG443 4.8 6.8 1.0 HB2 C:GLU15 4.9 7.1 1.0 HH12 C:ARG443 5.0 6.8 1.0 C C:CYS62 5.0 4.4 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.