Chlorine in PDB 8bgx: O-Methyltransferase PLU4890 in Complex with Sah and Aq-270A

The structure of O-Methyltransferase PLU4890 in Complex with Sah and Aq-270A, PDB code: 8bgx was solved by E.M.Huber, M.Groll, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	63.14, 78.37, 167.73, 90, 96.31, 90
R / Rfree (%)	17.9 / 22

The structure of O-Methyltransferase PLU4890 in Complex with Sah and Aq-270A also contains other interesting chemical elements:

Sodium

(Na)

5 atoms

The binding sites of Chlorine atom in the O-Methyltransferase PLU4890 in Complex with Sah and Aq-270A (pdb code 8bgx). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the O-Methyltransferase PLU4890 in Complex with Sah and Aq-270A, PDB code: 8bgx:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the O-Methyltransferase PLU4890 in Complex with Sah and Aq-270A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of O-Methyltransferase PLU4890 in Complex with Sah and Aq-270A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl406 b:67.7 occ:1.00 CD1 A:PHE268 3.5 30.5 1.0 CAT A:QPF402 3.5 68.4 1.0 CAR A:QPF402 3.7 65.7 1.0 NH2 D:ARG10 3.8 23.9 1.0 NH1 D:ARG10 3.9 24.6 1.0 OAS A:QPF402 3.9 73.4 1.0 CE A:MET88 4.0 33.0 1.0 CAA A:QPF402 4.1 67.4 1.0 CE1 A:PHE268 4.1 31.3 1.0 CG A:PHE268 4.2 28.8 1.0 CZ D:ARG10 4.3 23.6 1.0 CB A:PHE268 4.4 25.7 1.0 CAQ A:QPF402 4.4 61.5 1.0 CAB A:QPF402 4.7 63.1 1.0 CE A:MET258 4.7 48.7 1.0 CAC A:QPF402 4.8 60.7 1.0 SD A:MET88 4.9 31.2 1.0 CB D:THR3 5.0 33.8 1.0

Chlorine binding site 2 out of 4 in the O-Methyltransferase PLU4890 in Complex with Sah and Aq-270A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of O-Methyltransferase PLU4890 in Complex with Sah and Aq-270A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl407 b:59.5 occ:1.00 NH1 A:ARG10 3.4 26.6 1.0 NH2 A:ARG10 3.5 23.9 1.0 CD1 D:PHE268 3.5 28.1 1.0 CAT D:QPF402 3.7 68.5 1.0 CE D:MET88 3.8 35.2 1.0 CAR D:QPF402 3.8 65.4 1.0 OAS D:QPF402 3.8 69.1 1.0 CZ A:ARG10 3.9 24.6 1.0 CE1 D:PHE268 4.2 29.8 1.0 CG D:PHE268 4.2 26.4 1.0 CB D:PHE268 4.3 23.8 1.0 CAA D:QPF402 4.4 68.0 1.0 CAQ D:QPF402 4.6 63.1 1.0 CB A:THR3 4.9 33.2 1.0 O A:HOH588 4.9 34.8 1.0 SD D:MET88 5.0 32.9 1.0 OE2 A:GLU4 5.0 36.5 1.0

Chlorine binding site 3 out of 4 in the O-Methyltransferase PLU4890 in Complex with Sah and Aq-270A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of O-Methyltransferase PLU4890 in Complex with Sah and Aq-270A within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl403 b:62.7 occ:1.00 CD1 B:PHE268 3.4 43.1 1.0 CAT B:QPF402 3.6 72.7 1.0 CAR B:QPF402 3.7 69.1 1.0 OAS B:QPF402 3.8 74.2 1.0 CE B:MET88 3.8 48.0 1.0 CE1 B:PHE268 4.0 44.0 1.0 CAA B:QPF402 4.2 72.7 1.0 CG B:PHE268 4.3 41.2 1.0 CAQ B:QPF402 4.3 66.6 1.0 CB B:PHE268 4.5 38.0 1.0 SD B:MET88 4.8 44.6 1.0 CAB B:QPF402 4.8 70.3 1.0 CE B:MET258 4.8 59.5 1.0 CAC B:QPF402 4.9 66.6 1.0 O B:HOH563 5.0 42.1 1.0

Chlorine binding site 4 out of 4 in the O-Methyltransferase PLU4890 in Complex with Sah and Aq-270A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of O-Methyltransferase PLU4890 in Complex with Sah and Aq-270A within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl404 b:62.4 occ:1.00 CD1 C:PHE268 3.5 39.5 1.0 CE C:MET88 3.8 46.4 1.0 CAT C:QPF402 3.9 72.3 1.0 CE1 C:PHE268 4.1 40.9 1.0 CAR C:QPF402 4.2 72.5 1.0 CG C:PHE268 4.3 38.7 1.0 CAA C:QPF402 4.4 68.0 1.0 OAS C:QPF402 4.4 81.1 1.0 CB C:PHE268 4.4 36.2 1.0 CE C:MET258 4.8 63.2 1.0 CAQ C:QPF402 4.8 67.8 1.0 SD C:MET88 4.9 45.6 1.0

E.M.Huber, L.Kreling, A.K.Heinrich, M.Duennebacke, A.Poethig, H.B.Bode, M.Groll. A Set of Closely Related Methyltransferases For Site-Specific Tailoring of Anthraquinone Pigments Structure 2023.
ISSN: ISSN 0969-2126