Calcium in PDB 1fz8: Methane Monooxygenase Hydroxylase, Form II Cocrystallized with Dibromomethane

All present enzymatic activity of Methane Monooxygenase Hydroxylase, Form II Cocrystallized with Dibromomethane:
1.14.13.25;

The structure of Methane Monooxygenase Hydroxylase, Form II Cocrystallized with Dibromomethane, PDB code: 1fz8 was solved by D.A.Whittington, A.C.Rosenzweig, C.A.Frederick, S.J.Lippard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	23.50 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	71.170, 171.990, 221.330, 90.00, 90.00, 90.00
R / Rfree (%)	20.1 / 25

The structure of Methane Monooxygenase Hydroxylase, Form II Cocrystallized with Dibromomethane also contains other interesting chemical elements:

Bromine	(Br)	20 atoms
Iron	(Fe)	4 atoms

The binding sites of Calcium atom in the Methane Monooxygenase Hydroxylase, Form II Cocrystallized with Dibromomethane (pdb code 1fz8). 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 Cocrystallized with Dibromomethane, PDB code: 1fz8:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the Methane Monooxygenase Hydroxylase, Form II Cocrystallized with Dibromomethane


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 Cocrystallized with Dibromomethane within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca5005 b:35.7 occ:1.00 O A:HOH9113 2.4 25.1 1.0 OXT A:ASN527 2.5 34.5 1.0 O A:HOH9115 2.5 32.6 1.0 O A:HOH9114 2.6 29.3 1.0 O E:HOH216 2.7 32.3 1.0 C A:ASN527 3.4 31.7 1.0 CA A:ASN527 3.7 30.3 1.0 NH1 E:ARG162 4.0 36.0 1.0 O A:HOH9197 4.2 42.8 1.0 O A:ASN527 4.4 32.8 1.0 O A:PHE526 4.5 29.9 1.0 OE2 A:GLU440 4.5 46.8 1.0 CB A:ASN527 4.6 30.9 1.0 N A:ASN527 4.8 29.0 1.0 OE1 A:GLU440 4.8 48.7 1.0 O A:HOH9117 5.0 31.4 1.0

Calcium binding site 2 out of 3 in the Methane Monooxygenase Hydroxylase, Form II Cocrystallized with Dibromomethane


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 Cocrystallized with Dibromomethane within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca5006 b:50.2 occ:1.00 OD1 C:ASP348 2.4 34.9 1.0 O C:HOH9253 2.5 46.6 1.0 O C:HOH9139 2.6 25.8 1.0 O C:HOH9138 2.6 30.7 1.0 O C:HOH9140 2.8 48.0 1.0 CG C:ASP348 3.4 29.7 1.0 OD2 C:ASP348 3.8 31.5 1.0 OE1 C:GLU350 4.2 25.7 1.0 O C:HOH9242 4.3 32.2 1.0 O C:HOH9133 4.6 23.7 1.0 CB C:ASP348 4.8 23.7 1.0 CB C:GLU350 4.8 18.1 1.0 CD C:GLU350 5.0 29.0 1.0

Calcium binding site 3 out of 3 in the Methane Monooxygenase Hydroxylase, Form II Cocrystallized with Dibromomethane


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 Cocrystallized with Dibromomethane within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca5007 b:49.2 occ:1.00 OD1 C:ASP378 2.4 32.9 1.0 OD1 C:ASP376 2.6 28.7 1.0 OD2 C:ASP378 2.7 28.8 1.0 CG C:ASP378 2.9 28.1 1.0 OD2 C:ASP376 3.0 38.1 1.0 CG C:ASP376 3.1 31.2 1.0 CB C:ASP378 4.4 24.2 1.0 CB C:ASP376 4.5 26.7 1.0 O C:HOH9203 4.6 37.7 1.0 NE2 C:GLN379 4.7 50.2 1.0 O C:HOH9126 4.8 18.8 1.0 N C:ASP378 4.8 16.3 1.0 CA C:ASP376 5.0 23.4 1.0 N C:GLN379 5.0 18.8 1.0

D.A.Whittington, A.C.Rosenzweig, C.A.Frederick, S.J.Lippard. Xenon and Halogenated Alkanes Track Putative Substrate Binding Cavities in the Soluble Methane Monooxygenase Hydroxylase. Biochemistry V. 40 3476 2001.
ISSN: ISSN 0006-2960
PubMed: 11297413
DOI: 10.1021/BI0022487