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Molybdenum in PDB 1m34: Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate

Enzymatic activity of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate

All present enzymatic activity of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate:
1.18.6.1;

Protein crystallography data

The structure of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate, PDB code: 1m34 was solved by B.Schmid, O.Einsle, H.-J.Chiu, A.Willing, 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) 20.00 / 2.30
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 326.100, 75.800, 312.200, 90.00, 102.60, 90.00
R / Rfree (%) 20 / 23.6

Other elements in 1m34:

The structure of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate also contains other interesting chemical elements:

Fluorine (F) 32 atoms
Magnesium (Mg) 8 atoms
Aluminium (Al) 8 atoms
Iron (Fe) 76 atoms
Calcium (Ca) 4 atoms

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate (pdb code 1m34). 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 Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate, PDB code: 1m34:
Jump to Molybdenum binding site number: 1; 2; 3; 4;

Molybdenum binding site 1 out of 4 in 1m34

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Molybdenum binding site 1 out of 4 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mo2096

b:26.6
occ:1.00
 MO1 A:CFM2096 0.0 26.6 1.0
S3B A:CFM2096 2.3 23.4 1.0
S4B A:CFM2096 2.4 25.4 1.0
S1B A:CFM2096 2.4 24.5 1.0
FE6 A:CFM2096 2.7 21.1 1.0
FE5 A:CFM2096 2.9 25.5 1.0
FE7 A:CFM2096 2.9 20.4 1.0
O7 A:HCA2094 3.0 24.9 1.0
ND1 A:HIS442 3.0 25.3 1.0
O5 A:HCA2094 3.0 26.1 1.0
C7 A:HCA2094 3.4 28.6 1.0
C3 A:HCA2094 3.6 28.4 1.0
CE1 A:HIS442 3.9 26.9 1.0
C4 A:HCA2094 3.9 28.7 1.0
CG A:HIS442 3.9 26.3 1.0
CB A:HIS442 4.1 24.2 1.0
O1 A:HCA2094 4.3 23.9 1.0
O A:HOH2097 4.3 14.2 1.0
C2 A:HCA2094 4.5 27.9 1.0
O6 A:HCA2094 4.6 31.6 1.0
C1 A:HCA2094 4.7 28.0 1.0
CA A:HIS442 4.8 23.5 1.0
S2B A:CFM2096 4.8 20.1 1.0
O A:HOH2132 5.0 28.4 1.0
NE2 A:HIS442 5.0 31.4 1.0
FE3 A:CFM2096 5.0 22.7 1.0

Molybdenum binding site 2 out of 4 in 1m34

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Molybdenum binding site 2 out of 4 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mo2296

b:25.5
occ:1.00
 MO1 C:CFM2296 0.0 25.5 1.0
S4B C:CFM2296 2.3 25.0 1.0
S1B C:CFM2296 2.3 23.9 1.0
S3B C:CFM2296 2.4 22.6 1.0
FE7 C:CFM2296 2.7 21.2 1.0
FE6 C:CFM2296 2.7 24.6 1.0
FE5 C:CFM2296 2.8 25.0 1.0
ND1 C:HIS442 2.9 21.6 1.0
O5 C:HCA2294 2.9 22.7 1.0
O7 C:HCA2294 2.9 26.5 1.0
C7 C:HCA2294 3.6 28.4 1.0
CG C:HIS442 3.8 24.8 1.0
C3 C:HCA2294 3.8 29.5 1.0
CE1 C:HIS442 3.8 22.2 1.0
CB C:HIS442 3.9 25.2 1.0
O2 C:HCA2294 4.0 39.9 1.0
O C:HOH2306 4.3 23.1 1.0
C5 C:HCA2294 4.3 32.4 1.0
C1 C:HCA2294 4.5 34.3 1.0
CA C:HIS442 4.5 26.5 1.0
O6 C:HCA2294 4.7 30.7 1.0
C4 C:HCA2294 4.7 30.9 1.0
C2 C:HCA2294 4.8 32.7 1.0
S2B C:CFM2296 4.8 21.6 1.0
S5 C:CFM2296 4.9 22.0 1.0
NE2 C:HIS442 4.9 23.7 1.0
CD2 C:HIS442 4.9 23.9 1.0
S3A C:CFM2296 5.0 21.8 1.0
FE3 C:CFM2296 5.0 20.9 1.0

Molybdenum binding site 3 out of 4 in 1m34

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Molybdenum binding site 3 out of 4 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 3 of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Mo4096

b:22.9
occ:1.00
 MO1 I:CFM4096 0.0 22.9 1.0
S4B I:CFM4096 2.3 20.9 1.0
S1B I:CFM4096 2.3 21.8 1.0
S3B I:CFM4096 2.3 20.0 1.0
FE6 I:CFM4096 2.6 22.5 1.0
FE7 I:CFM4096 2.7 19.6 1.0
ND1 I:HIS442 2.7 17.0 1.0
FE5 I:CFM4096 2.7 19.6 1.0
O7 I:HCA4094 3.1 24.7 1.0
O5 I:HCA4094 3.1 25.6 1.0
C7 I:HCA4094 3.5 28.1 1.0
CE1 I:HIS442 3.6 18.4 1.0
C3 I:HCA4094 3.7 28.1 1.0
CG I:HIS442 3.7 19.9 1.0
CB I:HIS442 3.9 19.8 1.0
C4 I:HCA4094 4.0 28.4 1.0
O I:HOH4109 4.4 22.1 1.0
O1 I:HCA4094 4.4 23.4 1.0
CA I:HIS442 4.5 20.0 1.0
C2 I:HCA4094 4.6 27.8 1.0
O6 I:HCA4094 4.7 30.7 1.0
S2B I:CFM4096 4.7 22.6 1.0
NE2 I:HIS442 4.8 21.4 1.0
S5 I:CFM4096 4.8 18.9 1.0
CD2 I:HIS442 4.8 22.2 1.0
C1 I:HCA4094 4.9 27.4 1.0
FE3 I:CFM4096 4.9 20.2 1.0
S3A I:CFM4096 4.9 20.6 1.0

Molybdenum binding site 4 out of 4 in 1m34

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Molybdenum binding site 4 out of 4 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 4 of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate within 5.0Å range:
probe atom residue distance (Å) B Occ
K:Mo4296

b:27.3
occ:1.00
 MO1 K:CFM4296 0.0 27.3 1.0
S3B K:CFM4296 2.3 27.6 1.0
S4B K:CFM4296 2.3 29.2 1.0
S1B K:CFM4296 2.4 28.3 1.0
FE6 K:CFM4296 2.7 29.1 1.0
FE7 K:CFM4296 2.7 22.3 1.0
FE5 K:CFM4296 2.8 29.6 1.0
ND1 K:HIS442 2.9 29.0 1.0
O7 K:HCA4294 3.0 38.7 1.0
O5 K:HCA4294 3.2 38.3 1.0
C7 K:HCA4294 3.4 39.6 1.0
C3 K:HCA4294 3.6 38.8 1.0
CG K:HIS442 3.8 29.3 1.0
CE1 K:HIS442 3.9 28.6 1.0
CB K:HIS442 3.9 29.4 1.0
C4 K:HCA4294 4.0 39.7 1.0
O1 K:HCA4294 4.3 34.1 1.0
O K:HOH4299 4.3 20.6 1.0
C2 K:HCA4294 4.5 37.8 1.0
O6 K:HCA4294 4.6 42.9 1.0
CA K:HIS442 4.6 29.2 1.0
C1 K:HCA4294 4.8 35.7 1.0
S2B K:CFM4296 4.8 27.9 1.0
S5 K:CFM4296 4.9 23.0 1.0
NE2 K:HIS442 5.0 30.0 1.0

Reference:

B.Schmid, O.Einsle, H.-J.Chiu, A.Willing, M.Yoshida, J.B.Howard, D.C.Rees. Biochemical and Structural Characterization of the Crosslinked Complex of Nitrogenase: Comparison to the Adp-ALF4 Stabilized Structure Biochemistry V. 41 15557 2002.
ISSN: ISSN 0006-2960
PubMed: 12501184
DOI: 10.1021/BI026642B
Page generated: Sun Oct 6 15:24:23 2024

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