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Xenon in PDB 1fzi: Methane Monooxygenase Hydroxylase, Form I Pressurized with Xenon Gas

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

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

Protein crystallography data

The structure of Methane Monooxygenase Hydroxylase, Form I Pressurized with Xenon Gas, PDB code: 1fzi 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) 12.00 / 3.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 61.700, 109.600, 330.200, 90.00, 90.00, 90.00
R / Rfree (%) 22.3 / 25.3

Other elements in 1fzi:

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

Iron (Fe) 4 atoms

Xenon Binding Sites:

The binding sites of Xenon atom in the Methane Monooxygenase Hydroxylase, Form I Pressurized with Xenon Gas (pdb code 1fzi). This binding sites where shown within 5.0 Angstroms radius around Xenon atom.
In total 6 binding sites of Xenon where determined in the Methane Monooxygenase Hydroxylase, Form I Pressurized with Xenon Gas, PDB code: 1fzi:
Jump to Xenon binding site number: 1; 2; 3; 4; 5; 6;

Xenon binding site 1 out of 6 in 1fzi

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Xenon binding site 1 out of 6 in the Methane Monooxygenase Hydroxylase, Form I Pressurized with Xenon Gas


Mono view


Stereo pair view

A full contact list of Xenon with other atoms in the Xe binding site number 1 of Methane Monooxygenase Hydroxylase, Form I Pressurized with Xenon Gas within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Xe9001

b:10.2
occ:1.00
CB A:PHE109 3.9 0.0 1.0
SD A:MET184 4.1 15.5 1.0
CE A:MET184 4.2 17.8 1.0
CD2 A:LEU289 4.2 10.3 1.0
CD1 A:LEU286 4.3 21.6 1.0
O A:VAL106 4.5 8.6 1.0
CA A:VAL106 4.5 10.2 1.0
CE1 A:PHE282 4.6 0.1 1.0
CD2 A:PHE109 4.6 0.0 1.0
O A:VAL105 4.7 0.0 1.0
N A:LEU110 4.7 15.5 1.0
CG A:PHE109 4.7 0.0 1.0
CG1 A:VAL285 4.9 0.0 1.0
C A:PHE109 5.0 16.1 1.0
CG2 A:VAL106 5.0 0.0 1.0
XE A:XE9005 5.0 10.2 0.3

Xenon binding site 2 out of 6 in 1fzi

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Xenon binding site 2 out of 6 in the Methane Monooxygenase Hydroxylase, Form I Pressurized with Xenon Gas


Mono view


Stereo pair view

A full contact list of Xenon with other atoms in the Xe binding site number 2 of Methane Monooxygenase Hydroxylase, Form I Pressurized with Xenon Gas within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Xe9002

b:10.2
occ:1.00
CD2 B:LEU286 3.8 32.7 1.0
CD2 B:LEU289 4.0 8.6 1.0
CB B:PHE109 4.2 0.0 1.0
CE B:MET184 4.3 15.7 1.0
SD B:MET184 4.3 11.7 1.0
CA B:VAL106 4.5 10.1 1.0
CE1 B:PHE282 4.6 0.8 1.0
O B:VAL106 4.6 10.2 1.0
CD2 B:LEU216 4.8 49.1 1.0
N B:LEU110 4.9 5.0 1.0
O B:VAL105 4.9 0.0 1.0
CD2 B:PHE109 4.9 0.0 1.0
CG2 B:VAL106 5.0 0.0 1.0

Xenon binding site 3 out of 6 in 1fzi

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Xenon binding site 3 out of 6 in the Methane Monooxygenase Hydroxylase, Form I Pressurized with Xenon Gas


Mono view


Stereo pair view

A full contact list of Xenon with other atoms in the Xe binding site number 3 of Methane Monooxygenase Hydroxylase, Form I Pressurized with Xenon Gas within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Xe9003

b:15.2
occ:0.40
CD2 B:LEU361 3.7 0.0 1.0
CE1 B:TYR347 3.8 0.0 1.0
CA B:GLY293 3.9 4.0 1.0
N B:GLY293 4.0 5.4 1.0
CD1 B:LEU289 4.1 5.7 1.0
O B:MET288 4.1 0.5 1.0
C B:TYR292 4.1 3.8 1.0
O B:TYR292 4.2 6.1 1.0
CA B:LEU289 4.3 18.8 1.0
CD1 B:TYR347 4.4 0.0 1.0
CB B:TYR292 4.5 7.9 1.0
OG1 B:THR102 4.6 0.0 1.0
C B:MET288 4.6 0.8 1.0
CG B:MET288 4.7 14.8 1.0
O B:LEU289 4.7 18.0 1.0
CZ B:TYR347 4.8 0.0 1.0
N B:LEU289 4.8 17.2 1.0
OH B:TYR347 4.8 0.0 1.0
CA B:TYR292 4.9 3.8 1.0
C B:LEU289 5.0 17.9 1.0

Xenon binding site 4 out of 6 in 1fzi

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Xenon binding site 4 out of 6 in the Methane Monooxygenase Hydroxylase, Form I Pressurized with Xenon Gas


Mono view


Stereo pair view

A full contact list of Xenon with other atoms in the Xe binding site number 4 of Methane Monooxygenase Hydroxylase, Form I Pressurized with Xenon Gas within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Xe9004

b:10.2
occ:0.30
CD2 B:LEU478 3.6 1.1 1.0
CD2 B:LEU353 3.6 0.0 1.0
CG2 B:THR356 3.8 0.0 1.0
CD2 B:LEU405 3.9 0.0 1.0
CD1 B:LEU478 3.9 1.9 1.0
CZ B:PHE519 4.0 0.0 1.0
CE2 B:PHE519 4.2 0.0 1.0
CD B:PRO355 4.2 0.0 1.0
CA B:LEU353 4.2 9.9 1.0
CG B:LEU478 4.4 0.0 1.0
CG B:PRO355 4.4 0.0 1.0
CB B:PRO355 4.5 0.0 1.0
O B:LEU353 4.6 9.8 1.0
CB B:LEU353 4.6 0.0 1.0
SG B:CYS517 4.7 64.4 1.0
C B:LEU353 4.7 10.3 1.0
O B:ALA352 4.7 0.0 1.0
CG B:LEU353 4.8 0.0 1.0
CG2 B:ILE403 4.8 13.3 1.0
CB B:LEU405 4.9 0.0 1.0
CG B:LEU405 5.0 0.0 1.0

Xenon binding site 5 out of 6 in 1fzi

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Xenon binding site 5 out of 6 in the Methane Monooxygenase Hydroxylase, Form I Pressurized with Xenon Gas


Mono view


Stereo pair view

A full contact list of Xenon with other atoms in the Xe binding site number 5 of Methane Monooxygenase Hydroxylase, Form I Pressurized with Xenon Gas within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Xe9005

b:10.2
occ:0.30
CB A:LEU289 3.7 9.2 1.0
CE2 A:PHE290 3.7 1.5 1.0
CD1 A:LEU216 3.7 47.2 1.0
CD1 A:LEU286 3.7 21.6 1.0
CG2 A:VAL106 3.8 0.0 1.0
CZ A:PHE290 3.8 0.1 1.0
CG A:LEU286 4.0 25.7 1.0
CD2 A:PHE290 4.1 0.7 1.0
CD2 A:LEU289 4.1 10.3 1.0
O A:LEU286 4.2 0.0 1.0
CA A:LEU286 4.2 0.0 1.0
CG A:LEU289 4.2 12.5 1.0
CE1 A:PHE290 4.4 1.4 1.0
CG2 A:VAL220 4.5 4.0 1.0
CB A:LEU286 4.5 20.5 1.0
CG A:PHE290 4.6 0.0 1.0
C A:LEU286 4.7 0.0 1.0
CD1 A:PHE290 4.7 0.5 1.0
N A:PHE290 4.8 21.5 1.0
CG A:LEU216 4.8 48.0 1.0
CD2 A:LEU216 4.9 47.7 1.0
CA A:LEU289 4.9 0.0 1.0
CG1 A:VAL106 4.9 0.0 1.0
C A:LEU289 5.0 0.0 1.0
XE A:XE9001 5.0 10.2 1.0

Xenon binding site 6 out of 6 in 1fzi

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Xenon binding site 6 out of 6 in the Methane Monooxygenase Hydroxylase, Form I Pressurized with Xenon Gas


Mono view


Stereo pair view

A full contact list of Xenon with other atoms in the Xe binding site number 6 of Methane Monooxygenase Hydroxylase, Form I Pressurized with Xenon Gas within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Xe9006

b:15.2
occ:0.40
CE1 A:TYR347 3.7 0.0 1.0
CD1 A:LEU289 3.7 11.2 1.0
CD1 A:LEU361 3.8 14.1 1.0
O A:MET288 4.2 0.0 1.0
CA A:GLY293 4.2 12.2 1.0
CD1 A:TYR347 4.3 0.0 1.0
N A:GLY293 4.3 14.1 1.0
CA A:LEU289 4.4 0.0 1.0
C A:TYR292 4.5 0.0 1.0
CG A:MET288 4.5 0.0 1.0
CG A:LEU361 4.6 19.5 1.0
CB A:TYR292 4.7 28.3 1.0
O A:TYR292 4.7 0.0 1.0
C A:MET288 4.7 0.0 1.0
CZ A:TYR347 4.7 0.0 1.0
N A:LEU289 4.8 0.0 1.0
OG1 A:THR102 4.8 0.0 1.0
OH A:TYR347 4.9 0.0 1.0
O A:LEU289 5.0 0.0 1.0
CG A:LEU289 5.0 12.5 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: Wed Dec 16 02:39:23 2020

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