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Nickel 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:

Magnesium (Mg) 2 atoms
Iron (Fe) 20 atoms

Nickel Binding Sites:

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

Nickel binding site 1 out of 2 in 7uur

Go back to Nickel Binding Sites List in 7uur
Nickel 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 Nickel with other atoms in the Ni 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:Ni601

b:38.4
occ:1.00
O C:OH603 1.7 20.0 1.0
SG C:CYS62 2.1 9.2 1.0
SG C:CYS510 2.2 12.5 1.0
SG C:CYS513 2.6 10.6 1.0
FE C:FCO602 2.8 13.4 1.0
SG C:CYS65 2.9 9.1 1.0
CB C:CYS62 2.9 9.2 1.0
CB C:CYS510 3.1 12.5 1.0
CB C:CYS513 3.6 10.6 1.0
CG2 C:ILE64 3.7 8.8 1.0
C1 C:FCO602 3.8 13.4 1.0
CB C:CYS65 3.9 9.1 1.0
C2 C:FCO602 4.0 13.4 1.0
N C:CYS65 4.2 9.1 1.0
N C:CYS513 4.3 10.6 1.0
CA C:CYS62 4.3 9.2 1.0
CG2 C:VAL512 4.4 10.6 1.0
CA C:CYS513 4.4 10.6 1.0
C3 C:FCO602 4.5 13.4 1.0
CA C:CYS510 4.5 12.5 1.0
CD C:ARG443 4.5 11.4 1.0
CA C:CYS65 4.6 9.1 1.0
N1 C:FCO602 4.6 13.4 1.0
NH1 C:ARG443 4.8 11.4 1.0
NE C:ARG443 4.8 11.4 1.0
N2 C:FCO602 4.8 13.4 1.0
N C:ILE64 4.9 8.8 1.0
CZ C:ARG443 4.9 11.4 1.0
C C:CYS62 4.9 9.2 1.0
O C:CYS510 5.0 12.5 1.0
C C:CYS510 5.0 12.5 1.0
CB C:ILE64 5.0 8.8 1.0

Nickel binding site 2 out of 2 in 7uur

Go back to Nickel Binding Sites List in 7uur
Nickel 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 Nickel with other atoms in the Ni 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:Ni601

b:35.3
occ:1.00
O F:OH603 1.7 20.0 1.0
SG F:CYS62 2.1 9.0 1.0
SG F:CYS510 2.2 12.4 1.0
SG F:CYS513 2.6 10.6 1.0
FE F:FCO602 2.8 13.7 1.0
SG F:CYS65 2.9 9.0 1.0
CB F:CYS62 2.9 9.0 1.0
CB F:CYS510 3.1 12.4 1.0
CB F:CYS513 3.6 10.6 1.0
CG2 F:ILE64 3.7 8.8 1.0
C1 F:FCO602 3.8 13.7 1.0
CB F:CYS65 3.9 9.0 1.0
C2 F:FCO602 4.0 13.7 1.0
N F:CYS65 4.2 9.0 1.0
N F:CYS513 4.3 10.6 1.0
CA F:CYS62 4.3 9.0 1.0
CG2 F:VAL512 4.4 10.6 1.0
CA F:CYS513 4.5 10.6 1.0
C3 F:FCO602 4.5 13.7 1.0
CA F:CYS510 4.5 12.4 1.0
CD F:ARG443 4.5 11.4 1.0
CA F:CYS65 4.6 9.0 1.0
N1 F:FCO602 4.6 13.7 1.0
NH1 F:ARG443 4.8 11.4 1.0
NE F:ARG443 4.8 11.4 1.0
N2 F:FCO602 4.8 13.7 1.0
N F:ILE64 4.9 8.8 1.0
CZ F:ARG443 4.9 11.4 1.0
C F:CYS62 4.9 9.0 1.0
O F:CYS510 5.0 12.4 1.0
C F:CYS510 5.0 12.4 1.0
CB F:ILE64 5.0 8.8 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 10 09:27:30 2024

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