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Magnesium in PDB 3cur: Structure of A Double Methionine Mutant of Ni-Fe Hydrogenase

Enzymatic activity of Structure of A Double Methionine Mutant of Ni-Fe Hydrogenase

All present enzymatic activity of Structure of A Double Methionine Mutant of Ni-Fe Hydrogenase:
1.12.2.1;

Protein crystallography data

The structure of Structure of A Double Methionine Mutant of Ni-Fe Hydrogenase, PDB code: 3cur was solved by A.Volbeda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.99 / 2.40
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 64.600, 99.900, 183.000, 90.00, 91.60, 90.00
R / Rfree (%) 15 / 19.4

Other elements in 3cur:

The structure of Structure of A Double Methionine Mutant of Ni-Fe Hydrogenase also contains other interesting chemical elements:

Nickel (Ni) 3 atoms
Iron (Fe) 36 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of A Double Methionine Mutant of Ni-Fe Hydrogenase (pdb code 3cur). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Structure of A Double Methionine Mutant of Ni-Fe Hydrogenase, PDB code: 3cur:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 3cur

Go back to Magnesium Binding Sites List in 3cur
Magnesium binding site 1 out of 3 in the Structure of A Double Methionine Mutant of Ni-Fe Hydrogenase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of A Double Methionine Mutant of Ni-Fe Hydrogenase within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Mg553

b:39.0
occ:1.00
OE2 H:GLU53 2.0 40.2 1.0
O H:HOH566 2.1 40.2 1.0
O H:LEU495 2.1 38.7 1.0
O H:HOH564 2.1 37.8 1.0
O H:HOH565 2.1 38.1 1.0
NE2 H:HIS549 2.1 39.7 1.0
CD H:GLU53 3.0 41.0 1.0
CE1 H:HIS549 3.0 38.5 1.0
CD2 H:HIS549 3.2 39.9 1.0
C H:LEU495 3.2 39.6 1.0
OE1 H:GLU53 3.4 37.7 1.0
N H:LEU495 3.6 40.8 1.0
CA H:LEU495 3.9 40.1 1.0
OE2 H:GLU334 4.1 48.9 1.0
OE1 H:GLN494 4.1 42.1 1.0
CB H:LEU495 4.2 39.0 1.0
ND1 H:HIS549 4.2 39.3 1.0
OE1 H:GLU334 4.2 46.8 1.0
O H:HOH623 4.2 21.3 1.0
NZ H:LYS372 4.3 39.6 1.0
CG H:HIS549 4.3 42.6 1.0
O H:HOH578 4.3 29.8 1.0
N H:VAL496 4.3 40.1 1.0
CG H:GLU53 4.4 40.9 1.0
CD H:LYS372 4.4 40.5 1.0
CD H:GLU334 4.6 44.5 1.0
CE H:LYS372 4.6 41.6 1.0
C H:GLN494 4.7 40.8 1.0
CA H:VAL496 4.7 39.8 1.0
CA H:GLN494 4.9 40.1 1.0
O H:VAL548 5.0 40.9 1.0

Magnesium binding site 2 out of 3 in 3cur

Go back to Magnesium Binding Sites List in 3cur
Magnesium binding site 2 out of 3 in the Structure of A Double Methionine Mutant of Ni-Fe Hydrogenase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of A Double Methionine Mutant of Ni-Fe Hydrogenase within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Mg553

b:38.7
occ:1.00
OE2 I:GLU53 2.0 40.8 1.0
O I:HOH566 2.1 37.4 1.0
NE2 I:HIS549 2.1 40.2 1.0
O I:HOH565 2.1 36.9 1.0
O I:LEU495 2.1 39.2 1.0
O I:HOH567 2.2 39.8 1.0
CD I:GLU53 3.0 40.2 1.0
CE1 I:HIS549 3.0 38.3 1.0
CD2 I:HIS549 3.2 39.8 1.0
OE1 I:GLU53 3.3 40.0 1.0
C I:LEU495 3.3 39.8 1.0
N I:LEU495 3.7 40.5 1.0
CA I:LEU495 4.0 39.8 1.0
OE1 I:GLN494 4.1 42.5 1.0
ND1 I:HIS549 4.1 40.4 1.0
CB I:LEU495 4.2 39.6 1.0
OE2 I:GLU334 4.2 43.1 1.0
CG I:HIS549 4.3 42.8 1.0
OE1 I:GLU334 4.3 39.3 1.0
O I:HOH633 4.3 27.3 1.0
NZ I:LYS372 4.3 40.5 1.0
CG I:GLU53 4.3 39.5 1.0
O I:HOH578 4.4 23.2 1.0
N I:VAL496 4.4 40.7 1.0
CD I:LYS372 4.6 40.5 1.0
C I:GLN494 4.7 40.2 1.0
CD I:GLU334 4.7 41.6 1.0
CA I:VAL496 4.7 39.7 1.0
CE I:LYS372 4.8 41.9 1.0
CA I:GLN494 4.9 39.3 1.0

Magnesium binding site 3 out of 3 in 3cur

Go back to Magnesium Binding Sites List in 3cur
Magnesium binding site 3 out of 3 in the Structure of A Double Methionine Mutant of Ni-Fe Hydrogenase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structure of A Double Methionine Mutant of Ni-Fe Hydrogenase within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Mg553

b:38.0
occ:1.00
O J:HOH568 2.0 38.1 1.0
O J:HOH569 2.0 41.0 1.0
O J:HOH567 2.1 37.0 1.0
OE2 J:GLU53 2.1 40.9 1.0
O J:LEU495 2.1 39.4 1.0
NE2 J:HIS549 2.2 39.7 1.0
CD J:GLU53 3.1 40.2 1.0
CE1 J:HIS549 3.1 38.0 1.0
CD2 J:HIS549 3.2 41.1 1.0
C J:LEU495 3.3 40.4 1.0
OE1 J:GLU53 3.4 38.7 1.0
N J:LEU495 3.8 40.6 1.0
CA J:LEU495 4.0 39.4 1.0
OE2 J:GLU334 4.1 48.6 1.0
O J:HOH581 4.1 34.7 1.0
OE1 J:GLN494 4.1 41.9 1.0
OE1 J:GLU334 4.1 45.4 1.0
O J:HOH619 4.2 39.2 1.0
NZ J:LYS372 4.2 39.6 1.0
ND1 J:HIS549 4.3 39.5 1.0
CB J:LEU495 4.3 40.0 1.0
CG J:HIS549 4.3 42.5 1.0
N J:VAL496 4.4 40.7 1.0
CG J:GLU53 4.4 40.2 1.0
CD J:LYS372 4.5 40.2 1.0
CD J:GLU334 4.5 48.2 1.0
CE J:LYS372 4.7 41.3 1.0
CA J:VAL496 4.7 39.3 1.0
C J:GLN494 4.7 41.0 1.0
CA J:GLN494 5.0 40.6 1.0

Reference:

F.Leroux, S.Dementin, B.Burlat, L.Cournac, A.Volbeda, S.Champ, L.Martin, B.Guigliarelli, P.Bertrand, J.Fontecilla-Camps, M.Rousset. Experimental Approaches to Kinetics of Gas Diffusion in Hydrogenase Proc.Natl.Acad.Sci.Usa V. 105 11188 2008.
ISSN: ISSN 0027-8424
PubMed: 18685111
DOI: 10.1073/PNAS.0803689105
Page generated: Wed Aug 14 11:53:59 2024

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