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Calcium in PDB 1fzh: Methane Monooxygenase Hydroxylase, Form II Pressurized with Xenon Gas

Enzymatic activity of Methane Monooxygenase Hydroxylase, Form II Pressurized with Xenon Gas

All present enzymatic activity of Methane Monooxygenase Hydroxylase, Form II Pressurized with Xenon Gas:
1.14.13.25;

Protein crystallography data

The structure of Methane Monooxygenase Hydroxylase, Form II Pressurized with Xenon Gas, PDB code: 1fzh 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) 29.00 / 2.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 72.270, 174.620, 223.000, 90.00, 90.00, 90.00
R / Rfree (%) 20.6 / 26

Other elements in 1fzh:

The structure of Methane Monooxygenase Hydroxylase, Form II Pressurized with Xenon Gas also contains other interesting chemical elements:

Iron (Fe) 4 atoms
Xenon (Xe) 11 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Methane Monooxygenase Hydroxylase, Form II Pressurized with Xenon Gas (pdb code 1fzh). 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 II Pressurized with Xenon Gas, PDB code: 1fzh:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in 1fzh

Go back to Calcium Binding Sites List in 1fzh
Calcium binding site 1 out of 4 in the Methane Monooxygenase Hydroxylase, Form II Pressurized with Xenon Gas


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 Pressurized with Xenon Gas within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca5005

b:52.4
occ:1.00
OXT A:ASN527 2.6 33.9 1.0
C A:ASN527 3.6 33.4 1.0
CA A:ASN527 4.0 33.0 1.0
O A:PHE526 4.5 31.8 1.0
O A:ASN527 4.7 34.8 1.0
NH1 E:ARG162 4.7 48.2 1.0
OE1 A:GLU440 4.9 51.1 1.0
CB A:ASN527 5.0 33.1 1.0

Calcium binding site 2 out of 4 in 1fzh

Go back to Calcium Binding Sites List in 1fzh
Calcium binding site 2 out of 4 in the Methane Monooxygenase Hydroxylase, Form II Pressurized with Xenon Gas


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 Pressurized with Xenon Gas within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca5008

b:45.3
occ:1.00
OE1 B:GLN337 2.4 40.9 1.0
O B:HOH9142 2.6 37.4 1.0
OD1 B:ASP338 2.7 35.6 1.0
OD1 B:ASP334 2.8 44.4 1.0
OD2 B:ASP338 3.3 31.0 1.0
CG B:ASP338 3.4 32.8 1.0
CD B:GLN337 3.5 41.4 1.0
O B:HOH9139 3.7 23.6 1.0
CG B:ASP334 3.9 39.9 1.0
CG B:GLN337 4.2 41.8 1.0
OD2 B:ASP334 4.2 40.0 1.0
O B:HOH9076 4.2 26.0 1.0
NE2 B:GLN337 4.6 38.7 1.0
O B:ASP334 4.8 38.8 1.0
CB B:ASP338 4.9 32.7 1.0
O B:HOH9047 4.9 6.7 1.0

Calcium binding site 3 out of 4 in 1fzh

Go back to Calcium Binding Sites List in 1fzh
Calcium binding site 3 out of 4 in the Methane Monooxygenase Hydroxylase, Form II Pressurized with Xenon Gas


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 Pressurized with Xenon Gas within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ca5006

b:52.9
occ:1.00
OD1 C:ASP348 2.4 35.9 1.0
CG C:ASP348 3.5 32.6 1.0
OD2 C:ASP348 4.0 35.6 1.0
OE1 C:GLU350 4.2 35.3 1.0
CB C:ASP348 4.7 29.4 1.0
CB C:GLU350 4.8 26.0 1.0
CD C:GLU350 4.8 31.1 1.0

Calcium binding site 4 out of 4 in 1fzh

Go back to Calcium Binding Sites List in 1fzh
Calcium binding site 4 out of 4 in the Methane Monooxygenase Hydroxylase, Form II Pressurized with Xenon Gas


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 II Pressurized with Xenon Gas within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ca5007

b:70.5
occ:1.00
OE1 C:GLU222 2.6 38.7 1.0
CD C:GLU222 3.8 36.6 1.0
O C:HOH5083 4.0 21.1 1.0
O C:HOH5085 4.1 35.4 1.0
OD1 C:ASP334 4.1 31.2 1.0
OD2 C:ASP334 4.2 28.6 1.0
CG C:ASP334 4.2 29.1 1.0
O C:GLU222 4.3 30.0 1.0
CB C:GLU222 4.5 31.5 1.0
CG C:GLU222 4.6 35.0 1.0
OE2 C:GLU222 4.7 38.8 1.0
CD C:LYS225 4.9 23.7 1.0
CA C:GLU222 4.9 30.2 1.0

Reference:

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
Page generated: Sat Dec 12 02:56:51 2020

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