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Molybdenum in PDB 1m1n: Nitrogenase Mofe Protein From Azotobacter Vinelandii

Enzymatic activity of Nitrogenase Mofe Protein From Azotobacter Vinelandii

All present enzymatic activity of Nitrogenase Mofe Protein From Azotobacter Vinelandii:
1.18.6.1;

Protein crystallography data

The structure of Nitrogenase Mofe Protein From Azotobacter Vinelandii, PDB code: 1m1n was solved by O.Einsle, F.A.Tezcan, S.L.A.Andrade, B.Schmid, M.Yoshida, 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) 50.00 / 1.16
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 108.310, 131.630, 159.159, 90.00, 108.37, 90.00
R / Rfree (%) 12.3 / 14.9

Other elements in 1m1n:

The structure of Nitrogenase Mofe Protein From Azotobacter Vinelandii also contains other interesting chemical elements:

Iron (Fe) 60 atoms
Calcium (Ca) 4 atoms

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the Nitrogenase Mofe Protein From Azotobacter Vinelandii (pdb code 1m1n). 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 Azotobacter Vinelandii, PDB code: 1m1n:
Jump to Molybdenum binding site number: 1; 2; 3; 4;

Molybdenum binding site 1 out of 4 in 1m1n

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Molybdenum binding site 1 out of 4 in the Nitrogenase Mofe Protein From Azotobacter Vinelandii


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 Azotobacter Vinelandii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mo6496

b:12.4
occ:1.00
MO1 A:CFN6496 0.0 12.4 1.0
O5 A:HCA6494 2.2 11.5 1.0
O7 A:HCA6494 2.2 11.6 1.0
ND1 A:HIS442 2.3 11.4 1.0
S4B A:CFN6496 2.3 11.8 1.0
S1B A:CFN6496 2.3 12.2 1.0
S3B A:CFN6496 2.4 12.0 1.0
FE6 A:CFN6496 2.7 12.3 1.0
FE7 A:CFN6496 2.7 12.0 1.0
FE5 A:CFN6496 2.7 12.4 1.0
C7 A:HCA6494 3.1 11.7 1.0
C3 A:HCA6494 3.2 12.6 1.0
CE1 A:HIS442 3.3 11.8 1.0
CG A:HIS442 3.4 11.7 1.0
NX A:CFN6496 3.6 12.8 1.0
CB A:HIS442 3.7 12.8 1.0
C2 A:HCA6494 4.0 13.9 1.0
O A:HOH6640 4.1 15.7 1.0
C4 A:HCA6494 4.2 12.9 1.0
O6 A:HCA6494 4.3 11.8 1.0
O1 A:HCA6494 4.3 15.0 1.0
C5 A:HCA6494 4.3 12.5 1.0
NE2 A:HIS442 4.4 13.5 1.0
CD2 A:HIS442 4.5 12.7 1.0
CA A:HIS442 4.7 12.2 1.0
C1 A:HCA6494 4.7 14.4 1.0
S2B A:CFN6496 4.8 12.6 1.0
S5A A:CFN6496 4.8 12.4 1.0
S3A A:CFN6496 4.9 12.3 1.0

Molybdenum binding site 2 out of 4 in 1m1n

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Molybdenum binding site 2 out of 4 in the Nitrogenase Mofe Protein From Azotobacter Vinelandii


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 Azotobacter Vinelandii within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mo7496

b:11.2
occ:1.00
MO1 C:CFN7496 0.0 11.2 1.0
O5 C:HCA7494 2.2 10.2 1.0
O7 C:HCA7494 2.2 10.3 1.0
ND1 C:HIS442 2.3 10.8 1.0
S4B C:CFN7496 2.3 10.6 1.0
S1B C:CFN7496 2.3 10.6 1.0
S3B C:CFN7496 2.4 11.0 1.0
FE6 C:CFN7496 2.7 11.1 1.0
FE7 C:CFN7496 2.7 10.9 1.0
FE5 C:CFN7496 2.7 11.1 1.0
C7 C:HCA7494 3.1 11.9 1.0
C3 C:HCA7494 3.2 10.6 1.0
CE1 C:HIS442 3.2 10.4 1.0
CG C:HIS442 3.3 10.5 1.0
NX C:CFN7496 3.6 12.7 1.0
CB C:HIS442 3.7 11.1 1.0
C2 C:HCA7494 4.1 12.6 1.0
O C:HOH7581 4.2 13.8 1.0
C4 C:HCA7494 4.3 11.5 1.0
O6 C:HCA7494 4.3 11.4 1.0
C5 C:HCA7494 4.3 11.6 1.0
O1 C:HCA7494 4.3 13.9 1.0
NE2 C:HIS442 4.4 11.7 1.0
CD2 C:HIS442 4.5 10.5 1.0
CA C:HIS442 4.7 11.7 1.0
C1 C:HCA7494 4.7 13.3 1.0
S2B C:CFN7496 4.8 11.4 1.0
S5A C:CFN7496 4.8 11.6 1.0
S3A C:CFN7496 4.9 11.1 1.0

Molybdenum binding site 3 out of 4 in 1m1n

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Molybdenum binding site 3 out of 4 in the Nitrogenase Mofe Protein From Azotobacter Vinelandii


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 Azotobacter Vinelandii within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mo8496

b:13.9
occ:1.00
MO1 E:CFN8496 0.0 13.9 1.0
O5 E:HCA8494 2.2 13.0 1.0
O7 E:HCA8494 2.2 12.6 1.0
ND1 E:HIS442 2.3 13.8 1.0
S4B E:CFN8496 2.3 13.4 1.0
S1B E:CFN8496 2.3 13.9 1.0
S3B E:CFN8496 2.4 13.8 1.0
FE6 E:CFN8496 2.7 13.8 1.0
FE7 E:CFN8496 2.7 13.7 1.0
FE5 E:CFN8496 2.7 13.8 1.0
C7 E:HCA8494 3.1 14.6 1.0
C3 E:HCA8494 3.2 13.7 1.0
CE1 E:HIS442 3.2 12.7 1.0
CG E:HIS442 3.4 13.1 1.0
NX E:CFN8496 3.6 17.7 1.0
CB E:HIS442 3.7 13.1 1.0
C2 E:HCA8494 4.1 14.2 1.0
O E:HOH3220 4.2 15.9 1.0
C5 E:HCA8494 4.2 14.2 1.0
O6 E:HCA8494 4.3 13.4 1.0
C4 E:HCA8494 4.3 13.3 1.0
O1 E:HCA8494 4.3 15.9 1.0
NE2 E:HIS442 4.4 14.1 1.0
CD2 E:HIS442 4.5 14.2 1.0
CA E:HIS442 4.6 13.6 1.0
C1 E:HCA8494 4.7 15.7 1.0
S2B E:CFN8496 4.8 14.5 1.0
S5A E:CFN8496 4.8 14.6 1.0
S3A E:CFN8496 4.9 14.2 1.0

Molybdenum binding site 4 out of 4 in 1m1n

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Molybdenum binding site 4 out of 4 in the Nitrogenase Mofe Protein From Azotobacter Vinelandii


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 Azotobacter Vinelandii within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Mo9496

b:12.6
occ:1.00
MO1 G:CFN9496 0.0 12.6 1.0
O7 G:HCA9494 2.2 12.0 1.0
O5 G:HCA9494 2.2 11.1 1.0
ND1 G:HIS442 2.3 12.2 1.0
S4B G:CFN9496 2.3 11.9 1.0
S1B G:CFN9496 2.3 12.4 1.0
S3B G:CFN9496 2.4 12.4 1.0
FE6 G:CFN9496 2.7 12.4 1.0
FE7 G:CFN9496 2.7 12.1 1.0
FE5 G:CFN9496 2.7 12.6 1.0
C7 G:HCA9494 3.1 12.3 1.0
C3 G:HCA9494 3.2 12.5 1.0
CE1 G:HIS442 3.2 12.2 1.0
CG G:HIS442 3.4 11.6 1.0
NX G:CFN9496 3.6 13.2 1.0
CB G:HIS442 3.7 12.4 1.0
C2 G:HCA9494 4.1 14.2 1.0
O G:HOH2920 4.2 15.0 1.0
C4 G:HCA9494 4.3 13.2 1.0
C5 G:HCA9494 4.3 12.8 1.0
O1 G:HCA9494 4.3 15.6 1.0
O6 G:HCA9494 4.3 12.7 1.0
NE2 G:HIS442 4.4 13.3 1.0
CD2 G:HIS442 4.5 12.7 1.0
CA G:HIS442 4.6 12.3 1.0
C1 G:HCA9494 4.7 14.9 1.0
S2B G:CFN9496 4.8 12.8 1.0
S5A G:CFN9496 4.8 12.7 1.0
S3A G:CFN9496 4.9 12.5 1.0

Reference:

O.Einsle, F.A.Tezcan, S.L.Andrade, B.Schmid, M.Yoshida, J.B.Howard, D.C.Rees. Nitrogenase Mofe-Protein at 1.16 A Resolution: A Central Ligand in the Femo-Cofactor. Science V. 297 1696 2002.
ISSN: ISSN 0036-8075
PubMed: 12215645
DOI: 10.1126/SCIENCE.1073877
Page generated: Tue Dec 15 05:15:50 2020

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