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Nickel in PDB 1cc1: Crystal Structure of A Reduced, Active Form of the Ni-Fe-Se Hydrogenase From Desulfomicrobium Baculatum

Enzymatic activity of Crystal Structure of A Reduced, Active Form of the Ni-Fe-Se Hydrogenase From Desulfomicrobium Baculatum

All present enzymatic activity of Crystal Structure of A Reduced, Active Form of the Ni-Fe-Se Hydrogenase From Desulfomicrobium Baculatum:
1.18.99.1;

Protein crystallography data

The structure of Crystal Structure of A Reduced, Active Form of the Ni-Fe-Se Hydrogenase From Desulfomicrobium Baculatum, PDB code: 1cc1 was solved by E.Garcin, X.Vernede, E.C.Hatchikian, A.Volbeda, M.Frey, J.C.Fontecilla-Camps, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.15
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 110.390, 63.700, 99.580, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 24.8

Other elements in 1cc1:

The structure of Crystal Structure of A Reduced, Active Form of the Ni-Fe-Se Hydrogenase From Desulfomicrobium Baculatum also contains other interesting chemical elements:

Iron (Fe) 14 atoms

Nickel Binding Sites:

The binding sites of Nickel atom in the Crystal Structure of A Reduced, Active Form of the Ni-Fe-Se Hydrogenase From Desulfomicrobium Baculatum (pdb code 1cc1). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total only one binding site of Nickel was determined in the Crystal Structure of A Reduced, Active Form of the Ni-Fe-Se Hydrogenase From Desulfomicrobium Baculatum, PDB code: 1cc1:

Nickel binding site 1 out of 1 in 1cc1

Go back to Nickel Binding Sites List in 1cc1
Nickel binding site 1 out of 1 in the Crystal Structure of A Reduced, Active Form of the Ni-Fe-Se Hydrogenase From Desulfomicrobium Baculatum


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Crystal Structure of A Reduced, Active Form of the Ni-Fe-Se Hydrogenase From Desulfomicrobium Baculatum within 5.0Å range:
probe atom residue distance (Å) B Occ
L:Ni500

b:33.9
occ:1.00
 SG L:CYS70 2.3 28.1 1.0
SG L:CYS73 2.3 22.5 1.0
SE L:SEC492 2.5 45.5 1.0
FE L:FCO499 2.5 21.6 1.0
SG L:CYS495 2.6 21.9 1.0
CB L:CYS70 2.9 22.4 1.0
C2 L:FCO499 3.4 23.7 1.0
CB L:CYS73 3.5 18.1 1.0
CB L:SEC492 3.5 28.4 1.0
C1 L:FCO499 3.6 22.3 1.0
N L:CYS73 3.8 19.7 1.0
CB L:CYS495 4.0 19.3 1.0
C3 L:FCO499 4.2 29.0 1.0
CA L:CYS73 4.2 18.4 1.0
CA L:CYS70 4.4 20.4 1.0
N2 L:FCO499 4.4 20.7 1.0
CB L:VAL72 4.5 21.1 1.0
NH1 L:ARG425 4.5 27.7 1.0
N1 L:FCO499 4.5 16.7 1.0
CD L:ARG425 4.7 23.3 1.0
C L:VAL72 4.8 20.7 1.0
C L:CYS70 4.9 20.2 1.0
C L:CYS73 4.9 19.8 1.0
N L:CYS495 4.9 22.0 1.0
CA L:SEC492 4.9 23.6 1.0
N L:VAL72 4.9 20.7 1.0
CA L:CYS495 4.9 20.8 1.0
CZ L:ARG425 5.0 27.8 1.0
NE L:ARG425 5.0 25.9 1.0
CA L:VAL72 5.0 20.2 1.0
NE2 L:HIS77 5.0 17.5 1.0

Reference:

E.Garcin, X.Vernede, E.C.Hatchikian, A.Volbeda, M.Frey, J.C.Fontecilla-Camps. The Crystal Structure of A Reduced [Nifese] Hydrogenase Provides An Image of the Activated Catalytic Center Structure Fold.Des. V. 7 557 1999.
ISSN: ISSN 0969-2126
PubMed: 10378275
DOI: 10.1016/S0969-2126(99)80072-0
Page generated: Wed Oct 9 14:46:28 2024

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