Molybdenum in PDB 7opn: Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene

All present enzymatic activity of Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene:
1.2.3.1;

The structure of Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene, PDB code: 7opn was solved by C.Mota, C.Coelho, T.Santos Silva, M.J.Romao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.01 / 2.60
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	149.528, 149.528, 269.488, 90, 90, 90
R / Rfree (%)	20.6 / 24.1

The structure of Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene also contains other interesting chemical elements:

Iron

(Fe)

8 atoms

The binding sites of Molybdenum atom in the Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene (pdb code 7opn). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene, PDB code: 7opn:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in the Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene within 5.0Å range: probe atom residue distance (Å) B Occ A:Mo3004 b:67.8 occ:0.57 MO A:MOS3004 0.0 67.8 0.6 O2 A:MOS3004 1.9 62.1 0.6 O1 A:MOS3004 1.9 63.0 0.6 S A:MOS3004 2.3 63.7 0.6 S1' A:MTE3003 2.4 62.5 0.8 S2' A:MTE3003 2.4 68.8 0.8 C1' A:MTE3003 3.4 55.2 0.8 C2' A:MTE3003 3.4 59.3 0.8 O A:HOH3102 3.6 60.1 1.0 OE2 A:GLU1270 3.6 63.8 1.0 N A:GLY1088 3.8 64.3 1.0 CA A:GLY1087 4.1 54.4 1.0 CD A:GLU1270 4.1 64.4 1.0 C A:GLY1087 4.5 61.8 1.0 CG A:GLU1270 4.6 63.5 1.0 NE2 A:GLN776 4.6 49.9 1.0 N A:GLY808 4.6 48.8 1.0 CA A:GLY808 4.7 48.0 1.0 CA A:ARG921 4.7 58.9 1.0 OE1 A:GLU1270 4.8 67.4 1.0 N A:ARG921 4.8 54.8 1.0 CA A:GLY1088 4.8 64.6 1.0 O A:PHE920 4.8 56.3 1.0 C A:PHE920 4.9 54.6 1.0 C6 A:MTE3003 4.9 54.0 0.8 C3' A:MTE3003 4.9 56.7 0.8 C A:PHE807 5.0 49.4 1.0

Molybdenum binding site 2 out of 2 in the Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of Human Aldehyde Oxidase Snp R1231H in Complex with Raloxifene within 5.0Å range: probe atom residue distance (Å) B Occ B:Mo3004 b:76.5 occ:0.62 MO B:MOS3004 0.0 76.5 0.6 O2 B:MOS3004 1.9 69.9 0.6 O1 B:MOS3004 1.9 72.5 0.6 S B:MOS3004 2.3 70.9 0.6 S1' B:MTE3003 2.4 67.0 0.8 S2' B:MTE3003 2.4 71.1 0.8 O B:HOH3101 3.4 63.4 1.0 C1' B:MTE3003 3.4 61.7 0.8 C2' B:MTE3003 3.5 63.2 0.8 OE2 B:GLU1270 3.6 68.7 1.0 N B:GLY1088 3.9 68.7 1.0 CA B:GLY1087 4.1 62.6 1.0 CD B:GLU1270 4.1 68.7 1.0 C B:GLY1087 4.6 67.9 1.0 CA B:ARG921 4.6 62.7 1.0 CG B:GLU1270 4.6 67.0 1.0 N B:ARG921 4.6 58.2 1.0 N B:GLY808 4.7 50.0 1.0 CA B:GLY808 4.7 52.0 1.0 OE1 B:GLU1270 4.8 70.7 1.0 NE2 B:GLN776 4.9 48.1 1.0 CA B:GLY1088 4.9 68.4 1.0 C B:PHE920 4.9 59.0 1.0 C6 B:MTE3003 4.9 58.4 0.8 C3' B:MTE3003 4.9 61.6 0.8 O B:PHE920 4.9 61.8 1.0

C.Mota, A.Diniz, C.Coelho, T.Santos-Silva, M.Esmaeeli, S.Leimkuhler, E.J.Cabrita, F.Marcelo, M.J.Romao. Interrogating the Inhibition Mechanisms of Human Aldehyde Oxidase By X-Ray Crystallography and uc(Nmr) Spectroscopy: the Raloxifene Case. J.Med.Chem. 2021.
ISSN: ISSN 0022-2623
PubMed: 34415167
DOI: 10.1021/ACS.JMEDCHEM.1C01125