Atomistry » Nickel » PDB 7uur-7z5b » 7uur
Atomistry »
  Nickel »
    PDB 7uur-7z5b »
      7uur »

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

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy