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Magnesium in PDB 7uur: The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L)

Enzymatic activity of The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L)

All present enzymatic activity of The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L):
1.12.99.6;

Other elements in 7uur:

The structure of The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L) also contains other interesting chemical elements:

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

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L) (pdb code 7uur). 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 1.67 Angstrom Cryoem Structure of the [Nife]-Hydrogenase Huc From Mycobacterium Smegmatis - Catalytic Dimer (HUC2S2L), PDB code: 7uur:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 7uur

Go back to Magnesium Binding Sites List in 7uur
Magnesium binding site 1 out of 2 in the The 1.67 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 1.67 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:Mg604

b:11.1
occ:1.00
OE2 C:GLU43 1.9 10.8 1.0
O C:VAL462 2.0 10.0 1.0
NE2 C:HIS516 2.1 10.1 1.0
O C:HOH701 2.1 12.6 1.0
O C:HOH734 2.2 11.5 1.0
O C:HOH703 2.3 11.1 1.0
CD C:GLU43 2.9 10.8 1.0
CD2 C:HIS516 3.0 10.1 1.0
CE1 C:HIS516 3.1 10.1 1.0
C C:VAL462 3.2 10.0 1.0
OE1 C:GLU43 3.2 10.8 1.0
N C:VAL462 3.7 10.0 1.0
CA C:VAL462 3.9 10.0 1.0
OE2 C:GLU303 4.0 15.2 1.0
OE1 C:GLN461 4.0 11.6 1.0
OE1 C:GLU303 4.1 15.2 1.0
CG C:HIS516 4.2 10.1 1.0
ND1 C:HIS516 4.2 10.1 1.0
N C:VAL463 4.2 10.1 1.0
CG C:GLU43 4.2 10.8 1.0
O C:HOH774 4.2 11.7 1.0
CB C:VAL462 4.2 10.0 1.0
O C:HOH757 4.3 12.1 1.0
NZ C:LYS341 4.3 13.6 1.0
CD C:GLU303 4.5 15.2 1.0
CA C:VAL463 4.5 10.1 1.0
C C:GLN461 4.7 11.6 1.0
CE C:LYS341 4.8 13.6 1.0
CD C:LYS341 4.9 13.6 1.0
CG2 C:VAL463 4.9 10.1 1.0
CA C:GLN461 5.0 11.6 1.0
O C:VAL515 5.0 11.0 1.0

Magnesium binding site 2 out of 2 in 7uur

Go back to Magnesium Binding Sites List in 7uur
Magnesium binding site 2 out of 2 in the The 1.67 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 1.67 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
F:Mg604

b:11.1
occ:1.00
OE2 F:GLU43 2.0 10.8 1.0
O F:VAL462 2.0 10.0 1.0
NE2 F:HIS516 2.1 10.1 1.0
O F:HOH701 2.1 12.5 1.0
O F:HOH738 2.2 11.5 1.0
O F:HOH703 2.3 11.1 1.0
CD F:GLU43 2.9 10.8 1.0
CD2 F:HIS516 3.0 10.1 1.0
CE1 F:HIS516 3.1 10.1 1.0
C F:VAL462 3.2 10.0 1.0
OE1 F:GLU43 3.2 10.8 1.0
N F:VAL462 3.7 10.0 1.0
CA F:VAL462 3.9 10.0 1.0
OE2 F:GLU303 4.0 15.2 1.0
OE1 F:GLN461 4.0 11.6 1.0
OE1 F:GLU303 4.1 15.2 1.0
CG F:HIS516 4.2 10.1 1.0
ND1 F:HIS516 4.2 10.1 1.0
N F:VAL463 4.2 10.1 1.0
CG F:GLU43 4.2 10.8 1.0
CB F:VAL462 4.2 10.0 1.0
O F:HOH769 4.3 11.7 1.0
O F:HOH755 4.3 12.0 1.0
NZ F:LYS341 4.3 13.6 1.0
CA F:VAL463 4.5 10.1 1.0
CD F:GLU303 4.5 15.2 1.0
C F:GLN461 4.7 11.6 1.0
CE F:LYS341 4.8 13.6 1.0
CD F:LYS341 4.9 13.6 1.0
CG2 F:VAL463 4.9 10.1 1.0
O F:VAL515 5.0 11.1 1.0
CA F:GLN461 5.0 11.6 1.0

Reference:

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. An Oxygen-Insensitive, Quinone-Transporting Hydrogenase Enables Bacteria to Extract Energy From Air To Be Published.
Page generated: Thu Oct 3 10:13:36 2024

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