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Molybdenum in PDB 1fp4: Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase

Enzymatic activity of Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase

All present enzymatic activity of Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase:
1.18.6.1;

Protein crystallography data

The structure of Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase, PDB code: 1fp4 was solved by M.Sorlie, J.Christiansen, B.J.Lemon, J.W.Peters, D.R.Dean, B.J.Hales, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 107.200, 130.200, 80.400, 90.00, 111.20, 90.00
R / Rfree (%) 18.4 / 24

Other elements in 1fp4:

The structure of Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase 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 Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase (pdb code 1fp4). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase, PDB code: 1fp4:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in 1fp4

Go back to Molybdenum Binding Sites List in 1fp4
Molybdenum binding site 1 out of 2 in the Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mo496

b:27.8
occ:1.00
MO1 A:CFM496 0.0 27.8 1.0
O7 A:HCA494 2.2 29.4 1.0
O5 A:HCA494 2.2 25.9 1.0
ND1 A:HIS442 2.2 24.6 1.0
S4B A:CFM496 2.3 25.4 1.0
S1B A:CFM496 2.4 27.4 1.0
S3B A:CFM496 2.4 22.9 1.0
FE5 A:CFM496 2.8 26.6 1.0
FE7 A:CFM496 2.8 28.5 1.0
FE6 A:CFM496 2.8 28.0 1.0
CE1 A:HIS442 3.0 22.9 1.0
C7 A:HCA494 3.1 30.3 1.0
C3 A:HCA494 3.1 32.3 1.0
CG A:HIS442 3.2 20.9 1.0
CB A:HIS442 3.9 18.3 1.0
NE2 A:HIS442 4.1 22.1 1.0
C2 A:HCA494 4.1 32.1 1.0
C4 A:HCA494 4.2 29.7 1.0
O6 A:HCA494 4.2 30.7 1.0
CD2 A:HIS442 4.2 22.6 1.0
CA A:HIS442 4.5 19.9 1.0
O1 A:HCA494 4.5 32.8 1.0
C1 A:HCA494 4.8 34.4 1.0
C5 A:HCA494 4.8 26.8 1.0
S3A A:CFM496 5.0 29.2 1.0
CG2 A:ILE355 5.0 29.3 1.0
S5 A:CFM496 5.0 27.4 1.0

Molybdenum binding site 2 out of 2 in 1fp4

Go back to Molybdenum Binding Sites List in 1fp4
Molybdenum binding site 2 out of 2 in the Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mo497

b:28.4
occ:1.00
MO1 C:CFM497 0.0 28.4 1.0
O7 C:HCA495 2.2 30.1 1.0
O5 C:HCA495 2.2 26.5 1.0
ND1 C:HIS442 2.2 25.1 1.0
S3B C:CFM497 2.3 23.6 1.0
S1B C:CFM497 2.3 27.4 1.0
S4B C:CFM497 2.4 27.7 1.0
FE5 C:CFM497 2.8 30.0 1.0
FE7 C:CFM497 2.8 30.5 1.0
FE6 C:CFM497 2.9 29.8 1.0
CE1 C:HIS442 3.0 23.5 1.0
C7 C:HCA495 3.1 30.8 1.0
C3 C:HCA495 3.2 32.0 1.0
CG C:HIS442 3.2 22.2 1.0
CB C:HIS442 3.8 20.0 1.0
NE2 C:HIS442 4.1 23.7 1.0
C2 C:HCA495 4.1 32.2 1.0
C4 C:HCA495 4.2 29.1 1.0
CD2 C:HIS442 4.2 22.8 1.0
O6 C:HCA495 4.2 31.1 1.0
CA C:HIS442 4.4 19.9 1.0
O C:HOH555 4.5 56.3 1.0
O1 C:HCA495 4.6 32.8 1.0
C1 C:HCA495 4.9 34.4 1.0
C5 C:HCA495 4.9 26.5 1.0
CG2 C:ILE355 4.9 30.1 1.0
S5 C:CFM497 5.0 29.4 1.0
S3A C:CFM497 5.0 28.6 1.0

Reference:

M.Sorlie, J.Christiansen, B.J.Lemon, J.W.Peters, D.R.Dean, B.J.Hales. Mechanistic Features and Structure of the Nitrogenase Alpha-GLN195 Mofe Protein Biochemistry V. 40 1540 2001.
ISSN: ISSN 0006-2960
PubMed: 11327812
DOI: 10.1021/BI0013997
Page generated: Tue Dec 15 05:15:27 2020

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