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Molybdenum in PDB 8bts: Nitrogenase Mofe Protein From A. Vinelandii Alpha Double Mutant C45A/L158C

Enzymatic activity of Nitrogenase Mofe Protein From A. Vinelandii Alpha Double Mutant C45A/L158C

All present enzymatic activity of Nitrogenase Mofe Protein From A. Vinelandii Alpha Double Mutant C45A/L158C:
1.18.6.1;

Protein crystallography data

The structure of Nitrogenase Mofe Protein From A. Vinelandii Alpha Double Mutant C45A/L158C, PDB code: 8bts was solved by T.Wagner, N.Maslac, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 95.50 / 3.03
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 148.392, 73.444, 211.253, 90, 104.76, 90
R / Rfree (%) 20.4 / 22.3

Other elements in 8bts:

The structure of Nitrogenase Mofe Protein From A. Vinelandii Alpha Double Mutant C45A/L158C also contains other interesting chemical elements:

Iron (Fe) 64 atoms

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the Nitrogenase Mofe Protein From A. Vinelandii Alpha Double Mutant C45A/L158C (pdb code 8bts). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total 4 binding sites of Molybdenum where determined in the Nitrogenase Mofe Protein From A. Vinelandii Alpha Double Mutant C45A/L158C, PDB code: 8bts:
Jump to Molybdenum binding site number: 1; 2; 3; 4;

Molybdenum binding site 1 out of 4 in 8bts

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Molybdenum binding site 1 out of 4 in the Nitrogenase Mofe Protein From A. Vinelandii Alpha Double Mutant C45A/L158C


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Nitrogenase Mofe Protein From A. Vinelandii Alpha Double Mutant C45A/L158C within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mo602

b:12.3
occ:1.00
 MO1 A:ICS602 0.0 12.3 1.0
O7 A:HCA601 2.3 10.8 1.0
S1B A:ICS602 2.3 12.4 1.0
S4B A:ICS602 2.3 12.3 1.0
S3B A:ICS602 2.4 12.4 1.0
O6 A:HCA601 2.4 10.7 1.0
FE6 A:ICS602 2.6 12.4 1.0
ND1 A:HIS442 2.6 16.4 1.0
FE7 A:ICS602 2.7 12.4 1.0
FE5 A:ICS602 2.7 12.4 1.0
C7 A:HCA601 3.1 10.7 1.0
C3 A:HCA601 3.2 10.8 1.0
CE1 A:HIS442 3.4 16.9 1.0
CX A:ICS602 3.5 12.4 1.0
CG A:HIS442 3.7 14.7 1.0
CB A:HIS442 4.0 12.7 1.0
C2 A:HCA601 4.2 10.9 1.0
O2 A:HCA601 4.2 11.1 1.0
O5 A:HCA601 4.2 10.7 1.0
C4 A:HCA601 4.3 10.8 1.0
C5 A:HCA601 4.4 10.7 1.0
CA A:HIS442 4.6 11.9 1.0
NE2 A:HIS442 4.6 16.9 1.0
C1 A:HCA601 4.7 11.1 1.0
S2B A:ICS602 4.7 12.3 1.0
CD2 A:HIS442 4.8 15.8 1.0
S5A A:ICS602 4.8 12.4 1.0
S3A A:ICS602 4.9 12.6 1.0
FE2 A:ICS602 5.0 12.4 1.0

Molybdenum binding site 2 out of 4 in 8bts

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Molybdenum binding site 2 out of 4 in the Nitrogenase Mofe Protein From A. Vinelandii Alpha Double Mutant C45A/L158C


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of Nitrogenase Mofe Protein From A. Vinelandii Alpha Double Mutant C45A/L158C within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mo602

b:56.4
occ:1.00
 MO1 C:ICS602 0.0 56.4 1.0
S1B C:ICS602 2.3 56.2 1.0
S3B C:ICS602 2.4 56.4 1.0
S4B C:ICS602 2.4 56.3 1.0
O5 C:HCA601 2.5 36.3 1.0
FE6 C:ICS602 2.6 56.6 1.0
FE7 C:ICS602 2.7 56.4 1.0
ND1 C:HIS442 2.7 40.3 1.0
FE5 C:ICS602 2.8 56.3 1.0
O7 C:HCA601 2.8 36.3 1.0
C7 C:HCA601 3.3 36.4 1.0
CX C:ICS602 3.5 56.6 1.0
C3 C:HCA601 3.6 36.3 1.0
CG C:HIS442 3.6 38.4 1.0
CE1 C:HIS442 3.6 40.9 1.0
CB C:HIS442 3.8 35.9 1.0
O1 C:HCA601 4.2 36.3 1.0
O6 C:HCA601 4.3 36.5 1.0
C5 C:HCA601 4.5 36.2 1.0
C2 C:HCA601 4.6 36.3 1.0
CA C:HIS442 4.6 34.8 1.0
C4 C:HCA601 4.7 36.3 1.0
S2B C:ICS602 4.7 56.5 1.0
NE2 C:HIS442 4.8 40.8 1.0
CD2 C:HIS442 4.8 39.6 1.0
S5A C:ICS602 4.8 56.4 1.0
C1 C:HCA601 4.9 36.4 1.0
S3A C:ICS602 5.0 56.4 1.0

Molybdenum binding site 3 out of 4 in 8bts

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Molybdenum binding site 3 out of 4 in the Nitrogenase Mofe Protein From A. Vinelandii Alpha Double Mutant C45A/L158C


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 3 of Nitrogenase Mofe Protein From A. Vinelandii Alpha Double Mutant C45A/L158C within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Mo602

b:62.4
occ:1.00
 MO1 H:ICS602 0.0 62.4 1.0
S1B H:ICS602 2.3 62.2 1.0
S4B H:ICS602 2.4 62.4 1.0
S3B H:ICS602 2.4 62.4 1.0
O5 H:HCA601 2.5 51.5 1.0
O7 H:HCA601 2.7 51.5 1.0
FE5 H:ICS602 2.7 62.4 1.0
FE6 H:ICS602 2.7 62.4 1.0
FE7 H:ICS602 2.7 62.3 1.0
ND1 H:HIS442 2.8 39.8 1.0
C7 H:HCA601 3.4 51.5 1.0
CE1 H:HIS442 3.6 40.3 1.0
CX H:ICS602 3.6 62.2 1.0
C3 H:HCA601 3.6 51.6 1.0
CG H:HIS442 3.8 38.0 1.0
CB H:HIS442 4.1 35.7 1.0
C5 H:HCA601 4.3 51.6 1.0
C4 H:HCA601 4.5 51.6 1.0
O6 H:HCA601 4.5 51.6 1.0
O1 H:HCA601 4.7 51.6 1.0
C2 H:HCA601 4.7 51.6 1.0
NE2 H:HIS442 4.8 40.2 1.0
S2B H:ICS602 4.8 61.9 1.0
CA H:HIS442 4.9 34.8 1.0
S5A H:ICS602 4.9 62.2 1.0
S3A H:ICS602 4.9 62.6 1.0
CD2 H:HIS442 4.9 39.1 1.0

Molybdenum binding site 4 out of 4 in 8bts

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Molybdenum binding site 4 out of 4 in the Nitrogenase Mofe Protein From A. Vinelandii Alpha Double Mutant C45A/L158C


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 4 of Nitrogenase Mofe Protein From A. Vinelandii Alpha Double Mutant C45A/L158C within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Mo602

b:15.1
occ:1.00
 MO1 J:ICS602 0.0 15.1 1.0
O7 J:HCA601 2.3 16.6 1.0
S4B J:ICS602 2.3 15.4 1.0
S1B J:ICS602 2.3 15.2 1.0
O6 J:HCA601 2.4 16.6 1.0
S3B J:ICS602 2.4 15.3 1.0
FE7 J:ICS602 2.6 15.3 1.0
FE6 J:ICS602 2.6 15.3 1.0
FE5 J:ICS602 2.7 15.1 1.0
ND1 J:HIS442 2.7 24.4 1.0
C7 J:HCA601 3.1 16.7 1.0
C3 J:HCA601 3.2 16.6 1.0
CX J:ICS602 3.5 15.1 1.0
CE1 J:HIS442 3.7 24.9 1.0
CG J:HIS442 3.7 22.5 1.0
CB J:HIS442 3.9 19.9 1.0
O2 J:HCA601 4.1 16.4 1.0
C2 J:HCA601 4.2 16.5 1.0
C5 J:HCA601 4.2 16.4 1.0
C4 J:HCA601 4.3 16.5 1.0
O5 J:HCA601 4.3 16.8 1.0
C1 J:HCA601 4.6 16.5 1.0
CA J:HIS442 4.7 19.0 1.0
S5A J:ICS602 4.7 15.1 1.0
S2B J:ICS602 4.7 15.2 1.0
NE2 J:HIS442 4.8 24.9 1.0
CD2 J:HIS442 4.8 23.8 1.0
S3A J:ICS602 4.9 15.1 1.0
FE3 J:ICS602 5.0 15.2 1.0

Reference:

C.Cadoux, D.Ratcliff, N.Maslac, W.Gu, I.Tsakoumagkos, S.Hoogendoorn, T.Wagner, R.D.Milton. Nitrogen Fixation and Hydrogen Evolution By Sterically Encumbered Mo-Nitrogenase. Jacs Au V. 3 1521 2023.
ISSN: ESSN 2691-3704
PubMed: 37234119
DOI: 10.1021/JACSAU.3C00165
Page generated: Sun Oct 6 17:06:51 2024

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