Xenon in PDB 3mou: Characterization of the Inhibitor Binding Site of the Dehaloperoxidase-Hemoglobin From Amphitrite Ornata Using High- Pressure Xenon Derivatization

The structure of Characterization of the Inhibitor Binding Site of the Dehaloperoxidase-Hemoglobin From Amphitrite Ornata Using High- Pressure Xenon Derivatization, PDB code: 3mou was solved by V.S.De Serrano, S.Franzen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.51 / 1.71
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	57.945, 67.708, 68.359, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / 23

The structure of Characterization of the Inhibitor Binding Site of the Dehaloperoxidase-Hemoglobin From Amphitrite Ornata Using High- Pressure Xenon Derivatization also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Xenon atom in the Characterization of the Inhibitor Binding Site of the Dehaloperoxidase-Hemoglobin From Amphitrite Ornata Using High- Pressure Xenon Derivatization (pdb code 3mou). This binding sites where shown within 5.0 Angstroms radius around Xenon atom.
In total 4 binding sites of Xenon where determined in the Characterization of the Inhibitor Binding Site of the Dehaloperoxidase-Hemoglobin From Amphitrite Ornata Using High- Pressure Xenon Derivatization, PDB code: 3mou:
Jump to Xenon binding site number: 1; 2; 3; 4;

Xenon binding site 1 out of 4 in the Characterization of the Inhibitor Binding Site of the Dehaloperoxidase-Hemoglobin From Amphitrite Ornata Using High- Pressure Xenon Derivatization


Mono view


Stereo pair view

A full contact list of Xenon with other atoms in the Xe binding site number 1 of Characterization of the Inhibitor Binding Site of the Dehaloperoxidase-Hemoglobin From Amphitrite Ornata Using High- Pressure Xenon Derivatization within 5.0Å range: probe atom residue distance (Å) B Occ A:Xe181 b:13.1 occ:0.40 O A:HOH834 3.4 11.8 0.7 C1C A:HEM139 3.7 11.7 1.0 CE1 A:PHE21 3.8 12.4 1.0 C2C A:HEM139 3.8 10.9 1.0 CD1 A:PHE21 3.9 12.0 1.0 NC A:HEM139 4.0 11.7 1.0 CD2 A:LEU100 4.0 9.9 1.0 CHC A:HEM139 4.1 10.8 1.0 C3C A:HEM139 4.1 12.2 1.0 CE2 A:PHE24 4.2 9.6 1.0 CD1 A:LEU100 4.2 9.9 1.0 C4C A:HEM139 4.2 13.0 1.0 CZ A:PHE35 4.3 14.1 1.0 CG1 A:VAL59 4.3 10.5 1.0 CMC A:HEM139 4.3 10.0 1.0 CD2 A:PHE24 4.4 9.6 1.0 C4B A:HEM139 4.5 9.9 1.0 CG A:LEU100 4.7 9.2 1.0 FE A:HEM139 4.8 12.6 1.0 NB A:HEM139 4.9 10.7 1.0 CBC A:HEM139 4.9 16.0 1.0 CAC A:HEM139 5.0 14.2 1.0

Xenon binding site 2 out of 4 in the Characterization of the Inhibitor Binding Site of the Dehaloperoxidase-Hemoglobin From Amphitrite Ornata Using High- Pressure Xenon Derivatization


Mono view


Stereo pair view

A full contact list of Xenon with other atoms in the Xe binding site number 2 of Characterization of the Inhibitor Binding Site of the Dehaloperoxidase-Hemoglobin From Amphitrite Ornata Using High- Pressure Xenon Derivatization within 5.0Å range: probe atom residue distance (Å) B Occ A:Xe182 b:26.9 occ:0.10 O A:HOH338 3.3 15.3 1.0 O A:ASP79 3.4 12.4 1.0 CG2 A:VAL66 3.4 8.9 1.0 CD1 A:LEU62 3.5 9.9 1.0 CB A:THR82 3.6 17.1 1.0 CG2 A:THR82 3.6 17.4 1.0 OD2 A:ASP79 3.7 11.8 1.0 CG A:LEU62 3.9 8.5 1.0 CD2 A:LEU62 3.9 9.9 1.0 CA A:ASP79 3.9 12.4 1.0 CB A:ASP79 4.0 11.9 1.0 C A:ASP79 4.1 12.8 1.0 CG A:ASP79 4.1 12.1 1.0 CG A:LEU83 4.1 15.6 1.0 OG1 A:THR82 4.2 17.1 1.0 CD2 A:LEU83 4.3 14.7 1.0 NH2 A:ARG69 4.4 4.8 0.3 N A:LEU83 4.5 16.7 1.0 NH2 A:ARG69 4.7 4.7 0.4 CD1 A:LEU83 4.8 14.8 1.0 NH1 A:ARG69 4.8 13.3 0.3 CA A:THR82 4.8 17.2 1.0 C A:THR82 4.9 17.1 1.0 CB A:VAL66 4.9 7.5 1.0

Xenon binding site 3 out of 4 in the Characterization of the Inhibitor Binding Site of the Dehaloperoxidase-Hemoglobin From Amphitrite Ornata Using High- Pressure Xenon Derivatization


Mono view


Stereo pair view

A full contact list of Xenon with other atoms in the Xe binding site number 3 of Characterization of the Inhibitor Binding Site of the Dehaloperoxidase-Hemoglobin From Amphitrite Ornata Using High- Pressure Xenon Derivatization within 5.0Å range: probe atom residue distance (Å) B Occ B:Xe183 b:25.2 occ:0.20 CE1 B:PHE21 2.5 9.1 0.5 CZ B:PHE21 3.3 9.8 0.5 CD1 B:PHE21 3.4 9.0 0.5 O B:HOH835 3.4 7.8 0.7 CE1 B:PHE21 3.5 8.9 0.5 C1C B:HEM139 3.7 10.5 1.0 CD1 B:PHE21 3.8 9.0 0.5 C2C B:HEM139 3.9 11.1 1.0 CD2 B:LEU100 3.9 7.7 1.0 CHC B:HEM139 4.0 9.9 1.0 CG1 B:VAL59 4.0 7.6 0.6 NC B:HEM139 4.0 11.3 1.0 CG1 B:VAL59 4.1 7.6 0.4 CD1 B:LEU100 4.2 8.9 1.0 C3C B:HEM139 4.3 12.0 1.0 CMC B:HEM139 4.4 9.3 1.0 C4C B:HEM139 4.4 11.7 1.0 C4B B:HEM139 4.4 10.1 1.0 CZ B:PHE35 4.4 16.5 1.0 CE2 B:PHE24 4.5 8.5 1.0 CE2 B:PHE21 4.6 9.3 0.5 CD2 B:PHE24 4.6 9.6 1.0 CG B:LEU100 4.6 6.9 1.0 CG B:PHE21 4.7 7.9 0.5 CZ B:PHE21 4.7 9.3 0.5 CG2 B:VAL59 4.7 8.6 0.4 NB B:HEM139 4.7 10.0 1.0 CG2 B:VAL59 4.8 9.0 0.6 FE B:HEM139 4.8 10.6 1.0 CE1 B:HIS55 4.8 17.2 1.0 CE1 B:PHE35 4.9 16.0 1.0 CB B:VAL59 4.9 7.9 0.6 CB B:VAL59 5.0 7.9 0.4

Xenon binding site 4 out of 4 in the Characterization of the Inhibitor Binding Site of the Dehaloperoxidase-Hemoglobin From Amphitrite Ornata Using High- Pressure Xenon Derivatization


Mono view


Stereo pair view

A full contact list of Xenon with other atoms in the Xe binding site number 4 of Characterization of the Inhibitor Binding Site of the Dehaloperoxidase-Hemoglobin From Amphitrite Ornata Using High- Pressure Xenon Derivatization within 5.0Å range: probe atom residue distance (Å) B Occ B:Xe184 b:23.5 occ:0.30 OD2 B:ASP79 3.2 9.4 1.0 CD1 B:LEU62 3.5 9.0 1.0 O B:ASP79 3.5 8.7 1.0 O B:HOH392 3.6 27.0 1.0 CB B:THR82 3.7 11.9 1.0 CG2 B:VAL66 3.8 4.8 1.0 CG2 B:THR82 3.8 13.2 1.0 CA B:ASP79 3.8 8.5 1.0 CD2 B:LEU62 3.9 8.9 1.0 CG B:ASP79 3.9 8.6 1.0 CG B:LEU62 3.9 7.9 1.0 CB B:ASP79 4.0 8.1 1.0 C B:ASP79 4.1 8.5 1.0 CG B:LEU83 4.2 11.4 1.0 NH2 B:ARG69 4.4 8.8 1.0 OG1 B:THR82 4.4 13.4 1.0 CD2 B:LEU83 4.5 10.8 1.0 CD1 B:LEU83 4.7 11.7 1.0 N B:LEU83 4.7 11.1 1.0 CA B:THR82 4.9 11.8 1.0 OD1 B:ASP79 5.0 7.7 1.0

V.S.De Serrano, S.Franzen. Characterization of the Inhibitor Binding Site of the Dehaloperoxidase-Hemoglobin From Amphitrite Ornata Using High-Pressure Xenon Derivatization To Be Published.