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Calcium in PDB 1fz7: Methane Monooxygenase Hydroxylase, Form III Soaked in 0.9 M Ethanol

Enzymatic activity of Methane Monooxygenase Hydroxylase, Form III Soaked in 0.9 M Ethanol

All present enzymatic activity of Methane Monooxygenase Hydroxylase, Form III Soaked in 0.9 M Ethanol:
1.14.13.25;

Protein crystallography data

The structure of Methane Monooxygenase Hydroxylase, Form III Soaked in 0.9 M Ethanol, PDB code: 1fz7 was solved by D.A.Whittington, M.H.Sazinsky, S.J.Lippard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.96
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 71.400, 172.370, 221.130, 90.00, 90.00, 90.00
R / Rfree (%) 21.4 / 25.5

Other elements in 1fz7:

The structure of Methane Monooxygenase Hydroxylase, Form III Soaked in 0.9 M Ethanol also contains other interesting chemical elements:

Iron (Fe) 4 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Methane Monooxygenase Hydroxylase, Form III Soaked in 0.9 M Ethanol (pdb code 1fz7). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the Methane Monooxygenase Hydroxylase, Form III Soaked in 0.9 M Ethanol, PDB code: 1fz7:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in 1fz7

Go back to Calcium Binding Sites List in 1fz7
Calcium binding site 1 out of 3 in the Methane Monooxygenase Hydroxylase, Form III Soaked in 0.9 M Ethanol


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Methane Monooxygenase Hydroxylase, Form III Soaked in 0.9 M Ethanol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca5005

b:40.9
occ:1.00
OXT A:ASN527 2.3 39.6 1.0
O A:HOH9126 2.4 39.4 1.0
O A:HOH9088 2.5 34.0 1.0
O A:HOH9127 2.5 47.4 1.0
O A:HOH9087 2.5 29.6 1.0
O E:HOH484 2.5 40.9 1.0
C A:ASN527 3.4 36.3 1.0
CA A:ASN527 3.8 36.5 1.0
NH1 E:ARG162 4.1 42.7 1.0
O A:ASN527 4.5 36.0 1.0
OE2 A:GLU440 4.5 52.9 1.0
O A:PHE526 4.6 37.5 1.0
CB A:ASN527 4.8 35.9 1.0
N A:ASN527 4.9 36.0 1.0
OE1 A:GLU440 5.0 53.9 1.0

Calcium binding site 2 out of 3 in 1fz7

Go back to Calcium Binding Sites List in 1fz7
Calcium binding site 2 out of 3 in the Methane Monooxygenase Hydroxylase, Form III Soaked in 0.9 M Ethanol


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Methane Monooxygenase Hydroxylase, Form III Soaked in 0.9 M Ethanol within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ca5006

b:65.4
occ:1.00
O C:HOH5155 2.5 36.8 1.0
OD1 C:ASP348 2.5 44.3 1.0
O C:HOH5154 2.6 44.4 1.0
O C:HOH5152 2.8 59.8 1.0
O C:HOH5153 2.8 54.7 1.0
CG C:ASP348 3.6 38.9 1.0
OD2 C:ASP348 4.0 39.0 1.0
O C:HOH5291 4.2 57.4 1.0
OE1 C:GLU350 4.2 31.5 1.0
O C:HOH5234 4.4 54.1 1.0
O C:HOH5230 4.7 58.3 1.0
O C:HOH5059 4.7 27.7 1.0
CB C:GLU350 4.8 26.8 1.0
CB C:ASP348 4.8 29.6 1.0

Calcium binding site 3 out of 3 in 1fz7

Go back to Calcium Binding Sites List in 1fz7
Calcium binding site 3 out of 3 in the Methane Monooxygenase Hydroxylase, Form III Soaked in 0.9 M Ethanol


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Methane Monooxygenase Hydroxylase, Form III Soaked in 0.9 M Ethanol within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ca5007

b:40.5
occ:1.00
OE1 C:GLU222 2.2 43.5 1.0
O C:HOH5231 2.4 34.5 1.0
O C:HOH5019 2.5 35.2 1.0
O C:HOH5191 2.5 34.5 1.0
O C:HOH5190 2.9 37.8 1.0
CD C:GLU222 3.4 40.8 1.0
OE2 C:GLU222 4.3 44.4 1.0
CG C:GLU222 4.3 34.4 1.0
CB C:GLU222 4.4 28.6 1.0
OD1 C:ASP334 4.5 30.0 1.0
O C:HOH5011 4.5 29.3 1.0
OD2 C:ASP334 4.6 23.2 1.0
CD C:LYS225 4.6 30.7 1.0
CG C:ASP334 4.7 27.0 1.0
O C:GLU222 4.8 25.7 1.0
O C:HOH5020 4.9 25.6 1.0
CA C:GLU222 4.9 25.6 1.0

Reference:

D.A.Whittington, M.H.Sazinsky, S.J.Lippard. X-Ray Crystal Structure of Alcohol Products Bound at the Active Site of Soluble Methane Monooxygenase Hydroxylase. J.Am.Chem.Soc. V. 123 1794 2001.
ISSN: ISSN 0002-7863
PubMed: 11456795
DOI: 10.1021/JA0031725
Page generated: Mon Jul 7 15:00:10 2025

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