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Molybdenum in PDB 6o7l: Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling

Enzymatic activity of Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling

All present enzymatic activity of Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling:
1.18.6.1;

Protein crystallography data

The structure of Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling, PDB code: 6o7l was solved by H.L.Rutledge, F.A.Tezcan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.42 / 2.26
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 80.562, 131.029, 107.616, 90.00, 110.85, 90.00
R / Rfree (%) 20.8 / 25.4

Other elements in 6o7l:

The structure of Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling also contains other interesting chemical elements:

Iron (Fe) 32 atoms

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling (pdb code 6o7l). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling, PDB code: 6o7l:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in 6o7l

Go back to Molybdenum Binding Sites List in 6o7l
Molybdenum binding site 1 out of 2 in the Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mo502

b:37.9
occ:1.00
 MO1 A:ICS502 0.0 37.9 1.0
ND1 A:HIS442 2.2 38.0 1.0
S4B A:ICS502 2.3 36.5 1.0
S1B A:ICS502 2.4 37.0 1.0
S3B A:ICS502 2.4 34.8 1.0
O7 A:HCA501 2.4 38.4 1.0
O5 A:HCA501 2.5 39.3 1.0
FE6 A:ICS502 2.7 53.1 1.0
FE7 A:ICS502 2.7 50.4 1.0
FE5 A:ICS502 2.7 55.0 1.0
CE1 A:HIS442 3.0 31.1 1.0
HE1 A:HIS442 3.0 37.3 1.0
C7 A:HCA501 3.3 38.1 1.0
HB3 A:HIS442 3.3 45.1 1.0
C3 A:HCA501 3.4 43.5 1.0
CG A:HIS442 3.4 38.5 1.0
CX A:ICS502 3.5 44.8 1.0
H52 A:HCA501 3.6 46.9 1.0
CB A:HIS442 3.9 37.5 1.0
O A:HOH637 4.1 33.4 1.0
HA A:HIS442 4.1 42.8 1.0
NE2 A:HIS442 4.2 41.4 1.0
O1 A:HCA501 4.2 46.6 1.0
C4 A:HCA501 4.3 38.9 1.0
HD2 A:ARG96 4.4 49.4 1.0
CD2 A:HIS442 4.4 32.8 1.0
H22 A:HCA501 4.4 43.8 1.0
C2 A:HCA501 4.4 36.5 1.0
H41 A:HCA501 4.4 46.6 1.0
C5 A:HCA501 4.4 39.1 1.0
O6 A:HCA501 4.5 42.5 1.0
HG22 A:ILE355 4.5 55.2 1.0
CA A:HIS442 4.6 35.6 1.0
HH11 A:ARG96 4.6 55.1 1.0
HB2 A:HIS442 4.7 45.1 1.0
S2B A:ICS502 4.8 44.9 1.0
HD3 A:ARG96 4.8 49.4 1.0
S5A A:ICS502 4.8 37.4 1.0
C1 A:HCA501 4.8 42.2 1.0
HE2 A:HIS442 4.9 49.7 1.0
S3A A:ICS502 4.9 38.0 1.0
HA3 A:GLY356 5.0 53.7 1.0

Molybdenum binding site 2 out of 2 in 6o7l

Go back to Molybdenum Binding Sites List in 6o7l
Molybdenum binding site 2 out of 2 in the Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mo502

b:41.0
occ:1.00
 MO1 C:ICS502 0.0 41.0 1.0
S1B C:ICS502 2.3 44.5 1.0
S4B C:ICS502 2.3 41.0 1.0
S3B C:ICS502 2.4 36.4 1.0
O7 C:HCA501 2.4 43.7 1.0
ND1 C:HIS442 2.4 53.2 1.0
HD1 C:HIS442 2.5 63.9 1.0
O6 C:HCA501 2.5 44.7 1.0
CE1 C:HIS442 2.5 34.9 1.0
FE6 C:ICS502 2.7 57.2 1.0
HE1 C:HIS442 2.7 41.9 1.0
FE7 C:ICS502 2.7 52.4 1.0
FE5 C:ICS502 2.7 56.9 1.0
CG C:HIS442 3.1 42.9 1.0
NE2 C:HIS442 3.2 42.5 1.0
C7 C:HCA501 3.3 43.1 1.0
C3 C:HCA501 3.4 48.9 1.0
CX C:ICS502 3.5 43.5 1.0
CD2 C:HIS442 3.6 42.3 1.0
HB3 C:HIS442 3.8 52.7 1.0
CB C:HIS442 4.0 43.9 1.0
H41 C:HCA501 4.0 49.9 1.0
HA C:HIS442 4.1 49.5 1.0
O2 C:HCA501 4.2 49.9 1.0
C4 C:HCA501 4.3 41.6 1.0
HD2 C:HIS442 4.3 50.8 1.0
O5 C:HCA501 4.4 41.3 1.0
C2 C:HCA501 4.4 43.5 1.0
H22 C:HCA501 4.5 52.3 1.0
H52 C:HCA501 4.5 54.0 1.0
CA C:HIS442 4.6 41.2 1.0
HG22 C:ILE355 4.6 52.9 1.0
HE C:ARG96 4.7 54.2 1.0
S2B C:ICS502 4.8 47.9 1.0
S5A C:ICS502 4.8 42.7 1.0
C1 C:HCA501 4.8 45.4 1.0
HB2 C:HIS442 4.9 52.7 1.0
C5 C:HCA501 4.9 45.0 1.0
S3A C:ICS502 4.9 39.7 1.0
HA3 C:GLY356 4.9 60.2 1.0

Reference:

H.L.Rutledge, J.Rittle, L.M.Williamson, W.A.Xu, D.M.Gagnon, F.A.Tezcan. Redox-Dependent Metastability of the Nitrogenase P-Cluster. J.Am.Chem.Soc. V. 141 10091 2019.
ISSN: ESSN 1520-5126
PubMed: 31146522
DOI: 10.1021/JACS.9B04555
Page generated: Sun Oct 6 16:45:51 2024

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