Chlorine in PDB 2bxs: Human Monoamine Oxidase A in Complex with Clorgyline, Crystal Form B

All present enzymatic activity of Human Monoamine Oxidase A in Complex with Clorgyline, Crystal Form B:
1.4.3.4;

The structure of Human Monoamine Oxidase A in Complex with Clorgyline, Crystal Form B, PDB code: 2bxs was solved by L.De Colibus, C.Binda, D.E.Edmondson, A.Mattevi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 3.15
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	158.374, 152.076, 82.203, 90.00, 104.52, 90.00
R / Rfree (%)	26.8 / 33

The binding sites of Chlorine atom in the Human Monoamine Oxidase A in Complex with Clorgyline, Crystal Form B (pdb code 2bxs). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Human Monoamine Oxidase A in Complex with Clorgyline, Crystal Form B, PDB code: 2bxs:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Human Monoamine Oxidase A in Complex with Clorgyline, Crystal Form B


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human Monoamine Oxidase A in Complex with Clorgyline, Crystal Form B within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl601 b:62.9 occ:1.00 CL08 A:MLG601 0.0 62.9 1.0 C04 A:MLG601 1.7 59.8 1.0 C03 A:MLG601 2.6 59.9 1.0 C05 A:MLG601 2.6 61.7 1.0 SG A:CYS323 3.4 38.3 1.0 CD2 A:LEU337 3.4 37.8 1.0 C02 A:MLG601 3.8 60.9 1.0 C06 A:MLG601 3.9 62.1 1.0 CD1 A:ILE335 4.2 37.7 1.0 CG A:LEU337 4.2 38.1 1.0 O A:THR336 4.3 38.4 1.0 C01 A:MLG601 4.4 60.6 1.0 CG1 A:ILE335 4.5 38.0 1.0 CZ A:PHE208 4.6 38.9 1.0 CE1 A:PHE208 4.7 40.0 1.0 CB A:CYS323 4.8 38.0 1.0 CD1 A:LEU337 4.9 38.2 1.0 CD1 A:ILE325 5.0 36.3 1.0

Chlorine binding site 2 out of 4 in the Human Monoamine Oxidase A in Complex with Clorgyline, Crystal Form B


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Human Monoamine Oxidase A in Complex with Clorgyline, Crystal Form B within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl601 b:65.2 occ:1.00 CL07 A:MLG601 0.0 65.2 1.0 C02 A:MLG601 1.7 60.9 1.0 C03 A:MLG601 2.6 59.9 1.0 C01 A:MLG601 2.7 60.6 1.0 O09 A:MLG601 3.0 58.0 1.0 CG2 A:ILE335 3.0 36.5 1.0 CE2 A:PHE352 3.2 36.7 1.0 CD2 A:PHE352 3.4 37.3 1.0 C17 A:MLG601 3.6 46.0 1.0 C04 A:MLG601 3.8 59.8 1.0 CG1 A:ILE335 3.8 38.0 1.0 C06 A:MLG601 4.0 62.1 1.0 CB A:ILE335 4.0 37.0 1.0 CD1 A:ILE335 4.2 37.7 1.0 C10 A:MLG601 4.3 54.5 1.0 C05 A:MLG601 4.4 61.7 1.0 C12 A:MLG601 4.5 48.3 1.0 CZ A:PHE352 4.5 37.9 1.0 N13 A:MLG601 4.5 47.7 1.0 CG A:PHE352 4.7 37.6 1.0 CD1 A:LEU337 4.8 38.2 1.0 CG2 A:ILE180 4.9 37.1 1.0 CG A:LEU337 4.9 38.1 1.0 CE A:MET350 4.9 39.3 1.0 C A:ILE335 5.0 37.1 1.0

Chlorine binding site 3 out of 4 in the Human Monoamine Oxidase A in Complex with Clorgyline, Crystal Form B


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Human Monoamine Oxidase A in Complex with Clorgyline, Crystal Form B within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl601 b:63.2 occ:1.00 CL08 B:MLG601 0.0 63.2 1.0 C04 B:MLG601 1.7 61.3 1.0 C05 B:MLG601 2.6 62.7 1.0 C03 B:MLG601 2.7 59.4 1.0 SG B:CYS323 3.5 38.8 1.0 CD2 B:LEU337 3.7 37.9 1.0 C06 B:MLG601 3.9 61.8 1.0 C02 B:MLG601 4.0 61.1 1.0 CD1 B:ILE335 4.2 37.7 1.0 CZ B:PHE208 4.4 39.1 1.0 C01 B:MLG601 4.5 60.9 1.0 CE1 B:PHE208 4.5 40.0 1.0 O B:THR336 4.5 38.2 1.0 CG1 B:ILE335 4.6 38.2 1.0 CG B:LEU337 4.7 38.1 1.0 CD1 B:ILE325 4.7 36.6 1.0 CB B:CYS323 4.9 38.0 1.0

Chlorine binding site 4 out of 4 in the Human Monoamine Oxidase A in Complex with Clorgyline, Crystal Form B


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Human Monoamine Oxidase A in Complex with Clorgyline, Crystal Form B within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl601 b:64.0 occ:1.00 CL07 B:MLG601 0.0 64.0 1.0 C02 B:MLG601 1.7 61.1 1.0 C01 B:MLG601 2.5 60.9 1.0 O09 B:MLG601 2.7 59.9 1.0 C03 B:MLG601 2.7 59.4 1.0 C17 B:MLG601 3.0 49.5 1.0 CE2 B:PHE352 3.4 37.2 1.0 CG2 B:ILE335 3.6 36.4 1.0 CD2 B:PHE352 3.7 37.6 1.0 C06 B:MLG601 3.8 61.8 1.0 C04 B:MLG601 4.0 61.3 1.0 C12 B:MLG601 4.0 48.7 1.0 C10 B:MLG601 4.0 56.7 1.0 N13 B:MLG601 4.0 49.3 1.0 C05 B:MLG601 4.4 62.7 1.0 C11 B:MLG601 4.5 53.5 1.0 CG1 B:ILE335 4.5 38.2 1.0 CZ B:PHE352 4.6 38.1 1.0 CB B:ILE335 4.7 37.1 1.0 CD1 B:LEU337 4.7 38.2 1.0 CD1 B:ILE335 4.7 37.7 1.0 CG2 B:ILE180 4.7 37.0 1.0 CG B:LEU337 5.0 38.1 1.0

L.De Colibus, M.Li, C.Binda, A.Lustig, D.E.Edmondson, A.Mattevi. Three-Dimensional Structure of Human Monoamine Oxidase A (Mao A): Relation to the Structures of Rat Mao A and Human Mao B Proc.Natl.Acad.Sci.Usa V. 102 12864 2005.
ISSN: ISSN 0027-8424
PubMed: 16129825
DOI: 10.1073/PNAS.0505975102