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Molybdenum in PDB 6o7o: Nitrogenase Mofep Mutant F99Y/S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling

Enzymatic activity of Nitrogenase Mofep Mutant F99Y/S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling

All present enzymatic activity of Nitrogenase Mofep Mutant F99Y/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 F99Y/S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling, PDB code: 6o7o 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) 39.46 / 1.89
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 76.746, 128.678, 107.536, 90.00, 108.94, 90.00
R / Rfree (%) 14.9 / 18.6

Other elements in 6o7o:

The structure of Nitrogenase Mofep Mutant F99Y/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 F99Y/S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling (pdb code 6o7o). 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 F99Y/S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling, PDB code: 6o7o:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in 6o7o

Go back to Molybdenum Binding Sites List in 6o7o
Molybdenum binding site 1 out of 2 in the Nitrogenase Mofep Mutant F99Y/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 F99Y/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:16.0
occ:1.00
MO1 A:ICS502 0.0 16.0 1.0
O6 A:HCA501 2.2 13.1 1.0
O7 A:HCA501 2.3 13.3 1.0
S3B A:ICS502 2.3 14.4 1.0
ND1 A:HIS442 2.4 21.4 1.0
S1B A:ICS502 2.4 13.9 1.0
S4B A:ICS502 2.4 16.6 1.0
FE6 A:ICS502 2.7 17.9 1.0
FE7 A:ICS502 2.7 16.2 1.0
FE5 A:ICS502 2.7 16.4 1.0
C7 A:HCA501 3.1 19.0 1.0
CE1 A:HIS442 3.2 18.8 1.0
HB3 A:HIS442 3.2 19.2 1.0
C3 A:HCA501 3.2 16.0 1.0
HE1 A:HIS442 3.3 22.5 1.0
H52 A:HCA501 3.4 22.3 1.0
CG A:HIS442 3.4 16.4 1.0
CX A:ICS502 3.5 14.9 1.0
CB A:HIS442 3.8 16.0 1.0
H22 A:HCA501 4.0 20.8 1.0
O A:HOH765 4.1 20.3 1.0
C2 A:HCA501 4.2 17.3 1.0
O2 A:HCA501 4.2 19.1 1.0
HA A:HIS442 4.2 21.7 1.0
O5 A:HCA501 4.3 17.6 1.0
C5 A:HCA501 4.3 18.6 1.0
C4 A:HCA501 4.3 19.6 1.0
NE2 A:HIS442 4.4 19.5 1.0
HG22 A:ILE355 4.5 20.6 1.0
HE A:ARG96 4.5 25.1 1.0
CD2 A:HIS442 4.5 13.6 1.0
HB2 A:HIS442 4.6 19.2 1.0
H41 A:HCA501 4.6 23.6 1.0
CA A:HIS442 4.6 18.1 1.0
H51 A:HCA501 4.7 22.3 1.0
C1 A:HCA501 4.7 23.4 1.0
S2B A:ICS502 4.8 15.8 1.0
S5A A:ICS502 4.8 13.6 1.0
HA3 A:GLY356 4.9 21.7 1.0
S3A A:ICS502 4.9 19.0 1.0

Molybdenum binding site 2 out of 2 in 6o7o

Go back to Molybdenum Binding Sites List in 6o7o
Molybdenum binding site 2 out of 2 in the Nitrogenase Mofep Mutant F99Y/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 F99Y/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:15.6
occ:1.00
MO1 C:ICS502 0.0 15.6 1.0
O7 C:HCA501 2.2 19.4 1.0
O5 C:HCA501 2.2 15.4 1.0
S1B C:ICS502 2.3 14.2 1.0
S3B C:ICS502 2.4 12.9 1.0
S4B C:ICS502 2.4 15.6 1.0
ND1 C:HIS442 2.4 17.8 1.0
FE7 C:ICS502 2.6 17.0 1.0
FE6 C:ICS502 2.7 17.1 1.0
FE5 C:ICS502 2.7 19.1 1.0
C7 C:HCA501 3.1 18.9 1.0
HB3 C:HIS442 3.2 23.2 1.0
C3 C:HCA501 3.2 17.5 1.0
CE1 C:HIS442 3.2 20.0 1.0
HE1 C:HIS442 3.3 23.9 1.0
CG C:HIS442 3.4 16.0 1.0
H52 C:HCA501 3.5 24.4 1.0
CX C:ICS502 3.5 12.9 1.0
CB C:HIS442 3.8 19.4 1.0
H22 C:HCA501 3.9 22.1 1.0
O1 C:HCA501 4.1 23.4 1.0
C2 C:HCA501 4.1 18.4 1.0
HA C:HIS442 4.2 16.2 1.0
O6 C:HCA501 4.3 19.4 1.0
O C:HOH873 4.3 18.0 1.0
C4 C:HCA501 4.3 20.1 1.0
C5 C:HCA501 4.4 20.4 1.0
NE2 C:HIS442 4.4 19.4 1.0
HE C:ARG96 4.4 23.7 1.0
CD2 C:HIS442 4.5 18.6 1.0
HB2 C:HIS442 4.5 23.2 1.0
HG22 C:ILE355 4.6 23.3 1.0
H41 C:HCA501 4.6 24.1 1.0
CA C:HIS442 4.6 13.5 1.0
C1 C:HCA501 4.6 25.8 1.0
S5A C:ICS502 4.7 13.9 1.0
H51 C:HCA501 4.8 24.4 1.0
S2B C:ICS502 4.8 15.3 1.0
HA3 C:GLY356 4.9 20.0 1.0
S3A C:ICS502 4.9 16.4 1.0
HD2 C:ARG96 5.0 24.6 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: Tue Dec 15 05:20:47 2020

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