Calcium in PDB 1fz1: Methane Monooxygenase Hydroxylase, Form III Oxidized

All present enzymatic activity of Methane Monooxygenase Hydroxylase, Form III Oxidized:
1.14.13.25;

The structure of Methane Monooxygenase Hydroxylase, Form III Oxidized, PDB code: 1fz1 was solved by D.A.Whittington, S.J.Lippard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.80 / 1.96
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	71.400, 171.970, 221.380, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 23.4

The structure of Methane Monooxygenase Hydroxylase, Form III Oxidized also contains other interesting chemical elements:

Iron

(Fe)

4 atoms

The binding sites of Calcium atom in the Methane Monooxygenase Hydroxylase, Form III Oxidized (pdb code 1fz1). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the Methane Monooxygenase Hydroxylase, Form III Oxidized, PDB code: 1fz1:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in the Methane Monooxygenase Hydroxylase, Form III Oxidized


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 Oxidized within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca5005 b:37.5 occ:1.00 O A:HOH9244 2.4 29.9 1.0 O A:HOH9245 2.4 33.6 1.0 OXT A:ASN527 2.4 41.8 1.0 O A:HOH9246 2.4 26.1 1.0 O A:HOH9125 2.5 32.7 1.0 C A:ASN527 3.4 37.7 1.0 CA A:ASN527 3.8 35.8 1.0 NH1 E:ARG162 4.1 40.1 1.0 OE2 A:GLU440 4.3 45.7 1.0 O A:ASN527 4.4 39.1 1.0 O A:PHE526 4.5 33.7 1.0 CB A:ASN527 4.8 34.4 1.0 O A:HOH9209 4.8 42.8 1.0 N A:ASN527 4.9 33.2 1.0 OE1 A:GLU440 4.9 45.8 1.0 CD A:GLU440 5.0 42.6 1.0

Calcium binding site 2 out of 4 in the Methane Monooxygenase Hydroxylase, Form III Oxidized


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 Oxidized within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca5006 b:52.5 occ:1.00 OD1 C:ASP348 2.4 38.5 1.0 O C:HOH5266 2.5 50.7 1.0 O C:HOH5265 2.5 43.5 1.0 O C:HOH5261 2.6 28.3 1.0 O C:HOH5267 2.6 37.2 1.0 CG C:ASP348 3.5 32.9 1.0 O C:HOH5262 3.6 50.9 1.0 OD2 C:ASP348 3.9 32.6 1.0 OE1 C:GLU350 4.6 25.5 1.0 O C:HOH5268 4.6 33.3 1.0 O C:HOH5132 4.7 25.3 1.0 CB C:ASP348 4.8 27.2 1.0

Calcium binding site 3 out of 4 in the Methane Monooxygenase Hydroxylase, Form III Oxidized


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 Oxidized within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca5007 b:36.2 occ:1.00 OE1 C:GLU222 2.2 30.1 1.0 O C:HOH5227 2.4 34.2 1.0 O C:HOH5145 2.6 36.6 1.0 O C:HOH5291 2.9 46.2 1.0 CD C:GLU222 3.5 29.6 1.0 CG C:GLU222 4.2 25.3 1.0 CB C:GLU222 4.3 22.2 1.0 OE2 C:GLU222 4.4 36.2 1.0 OD1 C:ASP334 4.5 24.7 1.0 CD C:LYS225 4.5 32.3 1.0 OD2 C:ASP334 4.6 24.6 1.0 CG C:ASP334 4.7 23.5 1.0 O C:HOH5144 4.7 41.2 1.0 O C:HOH5043 4.7 25.0 1.0 O C:HOH5045 4.8 19.0 1.0 O C:GLU222 4.8 21.6 1.0 CA C:GLU222 4.9 19.7 1.0

Calcium binding site 4 out of 4 in the Methane Monooxygenase Hydroxylase, Form III Oxidized


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of Methane Monooxygenase Hydroxylase, Form III Oxidized within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca5008 b:44.5 occ:1.00 OD1 C:ASP378 2.4 29.0 1.0 O C:HOH5332 2.4 54.0 1.0 OD2 C:ASP378 2.5 26.1 1.0 OD1 C:ASP376 2.6 28.0 1.0 OD2 C:ASP376 2.7 38.5 1.0 O C:HOH5311 2.7 46.2 1.0 CG C:ASP378 2.8 26.6 1.0 CG C:ASP376 2.9 28.4 1.0 CB C:ASP378 4.3 22.0 1.0 CB C:ASP376 4.4 24.6 1.0 NE2 C:GLN379 4.5 48.4 1.0 N C:ASP378 4.6 16.6 1.0 O C:HOH5312 4.8 40.0 1.0 O C:HOH5136 4.8 18.3 1.0 CG C:GLN379 4.8 38.2 1.0 N C:GLN379 4.8 20.4 1.0 CA C:ASP376 4.9 23.5 1.0 CA C:ASP378 4.9 19.5 1.0

D.A.Whittington, S.J.Lippard. Crystal Structures of the Soluble Methane Monooxygenase Hydroxylase From Methylococcus Capsulatus (Bath) Demonstrating Geometrical Variability at the Dinuclear Iron Active Site. J.Am.Chem.Soc. V. 123 827 2001.
ISSN: ISSN 0002-7863
PubMed: 11456616
DOI: 10.1021/JA003240N