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Calcium in PDB 1fz0: Methane Monooxygenase Hydroxylase, Form II Mixed-Valent Grown Anaerobically

Enzymatic activity of Methane Monooxygenase Hydroxylase, Form II Mixed-Valent Grown Anaerobically

All present enzymatic activity of Methane Monooxygenase Hydroxylase, Form II Mixed-Valent Grown Anaerobically:
1.14.13.25;

Protein crystallography data

The structure of Methane Monooxygenase Hydroxylase, Form II Mixed-Valent Grown Anaerobically, PDB code: 1fz0 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) 30.00 / 2.07
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 71.420, 171.710, 221.490, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 23

Other elements in 1fz0:

The structure of Methane Monooxygenase Hydroxylase, Form II Mixed-Valent Grown Anaerobically 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 Mixed-Valent Grown Anaerobically (pdb code 1fz0). 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 Mixed-Valent Grown Anaerobically, PDB code: 1fz0:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in 1fz0

Go back to Calcium Binding Sites List in 1fz0
Calcium binding site 1 out of 3 in the Methane Monooxygenase Hydroxylase, Form II Mixed-Valent Grown Anaerobically


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 Mixed-Valent Grown Anaerobically within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca5005

b:35.5
occ:1.00
OXT A:ASN527 2.3 36.0 1.0
O A:HOH5147 2.4 33.6 1.0
O A:HOH5145 2.4 35.1 1.0
O A:HOH5146 2.5 29.7 1.0
O A:HOH5149 2.5 25.1 1.0
O A:HOH5148 2.7 33.6 1.0
C A:ASN527 3.3 34.5 1.0
CA A:ASN527 3.8 33.0 1.0
OE2 A:GLU440 4.2 48.3 1.0
NH1 E:ARG162 4.2 33.6 1.0
O A:ASN527 4.4 33.8 1.0
O A:PHE526 4.6 35.5 1.0
CB A:ASN527 4.8 33.8 1.0
N A:ASN527 4.9 32.8 1.0
O A:HOH5224 4.9 36.9 1.0
CD A:GLU440 5.0 42.7 1.0

Calcium binding site 2 out of 3 in 1fz0

Go back to Calcium Binding Sites List in 1fz0
Calcium binding site 2 out of 3 in the Methane Monooxygenase Hydroxylase, Form II Mixed-Valent Grown Anaerobically


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 Mixed-Valent Grown Anaerobically within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ca5006

b:46.9
occ:1.00
O C:HOH5171 2.4 47.6 1.0
O C:HOH5169 2.5 45.8 1.0
OD1 C:ASP348 2.5 36.1 1.0
O C:HOH5170 2.6 24.3 1.0
O C:HOH5162 2.7 30.0 1.0
CG C:ASP348 3.6 28.7 1.0
OD2 C:ASP348 4.0 30.9 1.0
O C:HOH5172 4.2 50.2 1.0
OE1 C:GLU350 4.5 23.5 1.0
O C:HOH5163 4.6 25.0 1.0
O C:HOH5239 4.6 30.1 1.0
CB C:ASP348 4.8 23.6 1.0
CB C:GLU350 4.9 20.7 1.0

Calcium binding site 3 out of 3 in 1fz0

Go back to Calcium Binding Sites List in 1fz0
Calcium binding site 3 out of 3 in the Methane Monooxygenase Hydroxylase, Form II Mixed-Valent Grown Anaerobically


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 Mixed-Valent Grown Anaerobically within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ca5007

b:51.0
occ:1.00
OD1 C:ASP378 2.5 26.4 1.0
OD1 C:ASP376 2.6 23.5 1.0
OD2 C:ASP378 2.6 28.0 1.0
OD2 C:ASP376 2.7 35.3 1.0
CG C:ASP378 2.9 26.4 1.0
CG C:ASP376 2.9 26.5 1.0
CB C:ASP378 4.4 24.0 1.0
CB C:ASP376 4.4 22.5 1.0
NE2 C:GLN379 4.6 48.7 1.0
N C:ASP378 4.7 17.3 1.0
CG C:GLN379 4.8 37.7 1.0
CA C:ASP376 4.9 22.1 1.0
N C:GLN379 4.9 18.5 1.0
O C:HOH5030 4.9 18.3 1.0

Reference:

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
Page generated: Sat Dec 12 02:56:29 2020

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