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Calcium in PDB 1fz6: Methane Monooxygenase Hydroxylase, Form II Soaked in 1 M Methanol

Enzymatic activity of Methane Monooxygenase Hydroxylase, Form II Soaked in 1 M Methanol

All present enzymatic activity of Methane Monooxygenase Hydroxylase, Form II Soaked in 1 M Methanol:
1.14.13.25;

Protein crystallography data

The structure of Methane Monooxygenase Hydroxylase, Form II Soaked in 1 M Methanol, PDB code: 1fz6 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) 29.90 / 2.05
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 70.670, 171.290, 221.340, 90.00, 90.00, 90.00
R / Rfree (%) 21.8 / 24.4

Other elements in 1fz6:

The structure of Methane Monooxygenase Hydroxylase, Form II Soaked in 1 M Methanol 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 II Soaked in 1 M Methanol (pdb code 1fz6). 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 II Soaked in 1 M Methanol, PDB code: 1fz6:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in 1fz6

Go back to Calcium Binding Sites List in 1fz6
Calcium binding site 1 out of 3 in the Methane Monooxygenase Hydroxylase, Form II Soaked in 1 M Methanol


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 II Soaked in 1 M Methanol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca5006

b:45.8
occ:1.00
O A:HOH5221 2.0 83.1 1.0
O A:HOH5161 2.2 34.3 1.0
OXT A:ASN527 2.3 35.5 1.0
O A:HOH5214 2.4 50.6 1.0
O A:HOH5216 2.5 40.6 1.0
O A:HOH5215 2.8 39.0 1.0
C A:ASN527 3.3 40.6 1.0
CA A:ASN527 3.8 39.6 1.0
O A:ASN527 4.4 42.0 1.0
O A:PHE526 4.4 39.7 1.0
NH1 E:ARG162 4.5 44.6 1.0
CB A:ASN527 4.7 39.6 1.0
OE1 A:GLU440 4.8 49.6 1.0
N A:ASN527 4.9 39.4 1.0

Calcium binding site 2 out of 3 in 1fz6

Go back to Calcium Binding Sites List in 1fz6
Calcium binding site 2 out of 3 in the Methane Monooxygenase Hydroxylase, Form II Soaked in 1 M Methanol


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 II Soaked in 1 M Methanol within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca5005

b:68.5
occ:1.00
OD1 B:ASP334 2.4 52.3 1.0
O B:HOH9195 2.7 54.8 1.0
OD1 B:ASP338 2.8 35.6 1.0
O B:HOH9204 2.9 45.5 1.0
O B:HOH9138 3.0 53.0 1.0
OE1 B:GLN337 3.1 51.6 1.0
CG B:ASP334 3.4 49.9 1.0
CG B:ASP338 3.6 35.6 1.0
OD2 B:ASP338 3.7 33.5 1.0
OD2 B:ASP334 3.8 52.8 1.0
O B:ASP334 4.2 41.7 1.0
CD B:GLN337 4.3 51.4 1.0
O B:HOH9099 4.4 28.4 1.0
CB B:ASP334 4.6 47.4 1.0
CA B:ASP334 4.7 45.1 1.0
CB B:GLN337 4.9 42.1 1.0
C B:ASP334 4.9 43.1 1.0

Calcium binding site 3 out of 3 in 1fz6

Go back to Calcium Binding Sites List in 1fz6
Calcium binding site 3 out of 3 in the Methane Monooxygenase Hydroxylase, Form II Soaked in 1 M Methanol


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 II Soaked in 1 M Methanol within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ca5007

b:77.1
occ:1.00
O C:HOH5240 2.1 57.5 1.0
OD1 C:ASP348 2.2 42.4 1.0
O C:HOH5239 2.4 68.6 1.0
O C:HOH5253 2.7 51.4 1.0
O C:HOH5254 2.8 42.1 1.0
O C:HOH5255 2.9 39.6 1.0
CG C:ASP348 3.4 38.0 1.0
OD2 C:ASP348 3.9 35.8 1.0
CB C:ASP348 4.5 32.7 1.0
O C:HOH5134 4.7 29.5 1.0
OE1 C:GLU350 4.8 31.3 1.0
O C:HOH5227 4.8 39.4 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: Thu Jul 11 08:21:13 2024

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