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Molybdenum in PDB 4tkv: Co-Bound Nitrogenase Mofe-Protein From A. Vinelandii

Enzymatic activity of Co-Bound Nitrogenase Mofe-Protein From A. Vinelandii

All present enzymatic activity of Co-Bound Nitrogenase Mofe-Protein From A. Vinelandii:
1.18.6.1;

Protein crystallography data

The structure of Co-Bound Nitrogenase Mofe-Protein From A. Vinelandii, PDB code: 4tkv was solved by T.Spatzal, K.Perez, O.Einsle, J.B.Howard, D.C.Rees, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.74 / 1.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 81.172, 130.623, 106.996, 90.00, 110.65, 90.00
R / Rfree (%) 13.8 / 15.4

Other elements in 4tkv:

The structure of Co-Bound Nitrogenase Mofe-Protein From A. Vinelandii also contains other interesting chemical elements:

Iron (Fe) 32 atoms

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the Co-Bound Nitrogenase Mofe-Protein From A. Vinelandii (pdb code 4tkv). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the Co-Bound Nitrogenase Mofe-Protein From A. Vinelandii, PDB code: 4tkv:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in 4tkv

Go back to Molybdenum Binding Sites List in 4tkv
Molybdenum binding site 1 out of 2 in the Co-Bound Nitrogenase Mofe-Protein From A. Vinelandii


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Co-Bound Nitrogenase Mofe-Protein From A. Vinelandii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mo502

b:11.4
occ:1.00
MO1 A:ICE502 0.0 11.4 1.0
O6 A:HCA501 2.2 11.1 1.0
O7 A:HCA501 2.2 12.2 1.0
S1B A:ICE502 2.3 11.2 1.0
S4B A:ICE502 2.3 11.9 1.0
S3B A:ICE502 2.4 11.9 1.0
ND1 A:HIS442 2.4 11.9 1.0
FE6 A:ICE502 2.6 11.6 1.0
FE7 A:ICE502 2.7 11.7 1.0
FE5 A:ICE502 2.7 11.9 1.0
C7 A:HCA501 3.0 11.5 1.0
C3 A:HCA501 3.2 10.7 1.0
CE1 A:HIS442 3.3 10.6 1.0
CG A:HIS442 3.4 10.9 1.0
CX A:ICE502 3.5 11.7 1.0
CB A:HIS442 3.7 11.1 1.0
C2 A:HCA501 4.1 11.1 1.0
O A:HOH657 4.2 13.9 1.0
O5 A:HCA501 4.2 11.4 1.0
C4 A:HCA501 4.3 10.5 1.0
C5 A:HCA501 4.3 10.7 1.0
O2 A:HCA501 4.4 14.2 1.0
C A:CMO504 4.4 11.8 1.0
NE2 A:HIS442 4.4 11.9 1.0
CD2 A:HIS442 4.5 11.1 1.0
CA A:HIS442 4.5 10.6 1.0
S5A A:ICE502 4.8 11.7 1.0
C1 A:HCA501 4.8 12.2 1.0
FE2 A:ICE502 4.9 11.7 1.0
S3A A:ICE502 4.9 12.2 1.0

Molybdenum binding site 2 out of 2 in 4tkv

Go back to Molybdenum Binding Sites List in 4tkv
Molybdenum binding site 2 out of 2 in the Co-Bound Nitrogenase Mofe-Protein From A. Vinelandii


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of Co-Bound Nitrogenase Mofe-Protein From A. Vinelandii within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mo502

b:11.7
occ:1.00
MO1 C:ICE502 0.0 11.7 1.0
O7 C:HCA501 2.2 10.6 1.0
O5 C:HCA501 2.2 11.7 1.0
S4B C:ICE502 2.3 11.8 1.0
S1B C:ICE502 2.3 11.6 1.0
S3B C:ICE502 2.3 12.0 1.0
ND1 C:HIS442 2.4 11.2 1.0
FE6 C:ICE502 2.6 11.8 1.0
FE7 C:ICE502 2.7 11.6 1.0
FE5 C:ICE502 2.7 12.4 1.0
C7 C:HCA501 3.0 11.3 1.0
C3 C:HCA501 3.2 11.0 1.0
CE1 C:HIS442 3.3 10.1 1.0
CG C:HIS442 3.4 11.0 1.0
CX C:ICE502 3.5 11.3 1.0
CB C:HIS442 3.7 11.1 1.0
C2 C:HCA501 4.1 11.5 1.0
O6 C:HCA501 4.2 11.7 1.0
O C:HOH645 4.2 13.1 1.0
C5 C:HCA501 4.3 9.7 1.0
C4 C:HCA501 4.3 10.0 1.0
C C:CMO504 4.4 10.4 1.0
O1 C:HCA501 4.4 13.7 1.0
NE2 C:HIS442 4.4 10.6 1.0
CD2 C:HIS442 4.5 11.0 1.0
CA C:HIS442 4.6 10.7 1.0
S5A C:ICE502 4.8 12.2 1.0
C1 C:HCA501 4.8 12.8 1.0
FE2 C:ICE502 4.9 11.7 1.0
S3A C:ICE502 4.9 11.8 1.0

Reference:

T.Spatzal, K.A.Perez, O.Einsle, J.B.Howard, D.C.Rees. Ligand Binding to the Femo-Cofactor: Structures of Co-Bound and Reactivated Nitrogenase. Science V. 345 1620 2014.
ISSN: ESSN 1095-9203
PubMed: 25258081
DOI: 10.1126/SCIENCE.1256679
Page generated: Tue Dec 15 05:19:12 2020

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