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Molybdenum in PDB 1mio: X-Ray Crystal Structure of the Nitrogenase Molybdenum-Iron Protein From Clostridium Pasteurianum at 3.0 Angstroms Resolution

Protein crystallography data

The structure of X-Ray Crystal Structure of the Nitrogenase Molybdenum-Iron Protein From Clostridium Pasteurianum at 3.0 Angstroms Resolution, PDB code: 1mio was solved by J.Kim, D.Woo, D.C.Rees, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 3.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 69.960, 151.300, 121.900, 90.00, 110.40, 90.00
R / Rfree (%) 18 / n/a

Other elements in 1mio:

The structure of X-Ray Crystal Structure of the Nitrogenase Molybdenum-Iron Protein From Clostridium Pasteurianum at 3.0 Angstroms Resolution also contains other interesting chemical elements:

Iron (Fe) 30 atoms
Calcium (Ca) 2 atoms

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the X-Ray Crystal Structure of the Nitrogenase Molybdenum-Iron Protein From Clostridium Pasteurianum at 3.0 Angstroms Resolution (pdb code 1mio). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the X-Ray Crystal Structure of the Nitrogenase Molybdenum-Iron Protein From Clostridium Pasteurianum at 3.0 Angstroms Resolution, PDB code: 1mio:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in 1mio

Go back to Molybdenum Binding Sites List in 1mio
Molybdenum binding site 1 out of 2 in the X-Ray Crystal Structure of the Nitrogenase Molybdenum-Iron Protein From Clostridium Pasteurianum at 3.0 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of X-Ray Crystal Structure of the Nitrogenase Molybdenum-Iron Protein From Clostridium Pasteurianum at 3.0 Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mo496

b:2.4
occ:1.00
MO1 B:CFM496 0.0 2.4 1.0
O7 B:HCA494 2.2 2.2 1.0
ND1 A:HIS482 2.2 3.5 1.0
O5 B:HCA494 2.2 2.1 1.0
S4B B:CFM496 2.3 5.1 1.0
S3B B:CFM496 2.3 3.2 1.0
S1B B:CFM496 2.4 7.8 1.0
FE6 B:CFM496 2.7 2.3 1.0
FE5 B:CFM496 2.8 5.0 1.0
FE7 B:CFM496 2.8 2.4 1.0
CE1 A:HIS482 2.9 4.1 1.0
C7 B:HCA494 3.1 2.0 1.0
C3 B:HCA494 3.2 2.0 1.0
CG A:HIS482 3.2 3.2 1.0
CB A:HIS482 3.9 2.8 1.0
C4 B:HCA494 4.0 2.1 1.0
NE2 A:HIS482 4.0 4.3 1.0
CD2 A:HIS482 4.2 3.9 1.0
O6 B:HCA494 4.3 5.1 1.0
C2 B:HCA494 4.4 2.9 1.0
CA A:HIS482 4.6 3.0 1.0
C1 B:HCA494 4.7 2.0 1.0
O2 B:HCA494 4.8 2.1 1.0
C5 B:HCA494 4.9 2.1 1.0
S2B B:CFM496 4.9 9.0 1.0
S5 B:CFM496 5.0 2.1 1.0
S3A B:CFM496 5.0 5.2 1.0

Molybdenum binding site 2 out of 2 in 1mio

Go back to Molybdenum Binding Sites List in 1mio
Molybdenum binding site 2 out of 2 in the X-Ray Crystal Structure of the Nitrogenase Molybdenum-Iron Protein From Clostridium Pasteurianum at 3.0 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of X-Ray Crystal Structure of the Nitrogenase Molybdenum-Iron Protein From Clostridium Pasteurianum at 3.0 Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mo496

b:7.2
occ:1.00
MO1 D:CFM496 0.0 7.2 1.0
O5 D:HCA494 2.2 8.9 1.0
O7 D:HCA494 2.2 8.1 1.0
ND1 C:HIS482 2.2 9.6 1.0
S4B D:CFM496 2.3 9.8 1.0
S3B D:CFM496 2.4 2.2 1.0
S1B D:CFM496 2.4 3.0 1.0
FE7 D:CFM496 2.7 2.4 1.0
FE5 D:CFM496 2.8 2.2 1.0
FE6 D:CFM496 2.9 23.8 1.0
CE1 C:HIS482 3.0 8.8 1.0
C7 D:HCA494 3.1 10.0 1.0
C3 D:HCA494 3.2 8.7 1.0
CG C:HIS482 3.3 9.9 1.0
CB C:HIS482 4.0 8.6 1.0
C2 D:HCA494 4.2 8.9 1.0
NE2 C:HIS482 4.2 10.5 1.0
O6 D:HCA494 4.2 17.1 1.0
C4 D:HCA494 4.3 11.7 1.0
C5 D:HCA494 4.3 12.7 1.0
CD2 C:HIS482 4.4 11.2 1.0
O2 D:HCA494 4.5 10.9 1.0
CA C:HIS482 4.6 8.0 1.0
FE4 D:CFM496 4.9 2.1 1.0
S3A D:CFM496 4.9 7.1 1.0
C1 D:HCA494 4.9 8.6 1.0
S5 D:CFM496 4.9 4.1 1.0
CG1 C:VAL343 5.0 13.6 1.0

Reference:

J.Kim, D.Woo, D.C.Rees. X-Ray Crystal Structure of the Nitrogenase Molybdenum-Iron Protein From Clostridium Pasteurianum at 3.0-A Resolution. Biochemistry V. 32 7104 1993.
ISSN: ISSN 0006-2960
PubMed: 8393705
DOI: 10.1021/BI00079A006
Page generated: Tue Dec 15 05:15:54 2020

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