Manganese in PDB 6qeh: Crystal Structure of Human Methionine Aminopeptidase-2 in Complex with An Inhibitor 5-Chloro-Quinolin-8-Ol

All present enzymatic activity of Crystal Structure of Human Methionine Aminopeptidase-2 in Complex with An Inhibitor 5-Chloro-Quinolin-8-Ol:
3.4.11.18;

The structure of Crystal Structure of Human Methionine Aminopeptidase-2 in Complex with An Inhibitor 5-Chloro-Quinolin-8-Ol, PDB code: 6qeh was solved by D.Musil, T.Heinrich, M.Lehmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.01 / 2.17
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	90.060, 100.260, 100.340, 90.00, 90.00, 90.00
R / Rfree (%)	18.4 / 22

The structure of Crystal Structure of Human Methionine Aminopeptidase-2 in Complex with An Inhibitor 5-Chloro-Quinolin-8-Ol also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Manganese atom in the Crystal Structure of Human Methionine Aminopeptidase-2 in Complex with An Inhibitor 5-Chloro-Quinolin-8-Ol (pdb code 6qeh). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of Human Methionine Aminopeptidase-2 in Complex with An Inhibitor 5-Chloro-Quinolin-8-Ol, PDB code: 6qeh:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of Human Methionine Aminopeptidase-2 in Complex with An Inhibitor 5-Chloro-Quinolin-8-Ol


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Human Methionine Aminopeptidase-2 in Complex with An Inhibitor 5-Chloro-Quinolin-8-Ol within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn503 b:32.4 occ:1.00 OD2 A:ASP262 2.1 29.6 1.0 O11 A:HZQ502 2.3 41.5 1.0 OE2 A:GLU364 2.3 47.6 1.0 NE2 A:HIS331 2.4 32.9 1.0 OE2 A:GLU459 2.4 28.0 1.0 N6 A:HZQ502 2.6 37.9 1.0 CG A:ASP262 3.1 30.8 1.0 CD A:GLU364 3.1 45.6 1.0 C5 A:HZQ502 3.2 40.2 1.0 C2 A:HZQ502 3.3 39.5 1.0 CD2 A:HIS331 3.3 33.3 1.0 CD A:GLU459 3.4 29.8 1.0 CE1 A:HIS331 3.4 32.8 1.0 MN A:MN504 3.4 26.6 1.0 OD1 A:ASP262 3.4 32.0 1.0 OE1 A:GLU364 3.5 36.3 1.0 OE1 A:GLU459 3.6 21.8 1.0 C12 A:HZQ502 3.6 37.7 1.0 O A:HOH725 3.8 37.4 1.0 CB A:ALA362 4.2 30.0 1.0 CG A:GLU364 4.2 35.8 1.0 CB A:ASP262 4.4 25.1 1.0 C10 A:HZQ502 4.5 38.3 1.0 CG A:HIS331 4.5 32.6 1.0 ND1 A:HIS331 4.5 33.3 1.0 O A:HOH664 4.6 54.0 1.0 C1 A:HZQ502 4.7 39.1 1.0 CG A:GLU459 4.8 35.4 1.0 C9 A:HZQ502 4.9 36.0 1.0 CG1 A:ILE338 5.0 33.4 1.0 CD1 A:ILE338 5.0 36.1 1.0 OD2 A:ASP251 5.0 20.6 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of Human Methionine Aminopeptidase-2 in Complex with An Inhibitor 5-Chloro-Quinolin-8-Ol


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Human Methionine Aminopeptidase-2 in Complex with An Inhibitor 5-Chloro-Quinolin-8-Ol within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn504 b:26.6 occ:1.00 OD1 A:ASP262 2.0 32.0 1.0 OD1 A:ASP251 2.1 16.4 1.0 OE1 A:GLU459 2.1 21.8 1.0 O11 A:HZQ502 2.1 41.5 1.0 OD2 A:ASP251 2.3 20.6 1.0 CG A:ASP251 2.5 15.1 1.0 CG A:ASP262 3.1 30.8 1.0 CD A:GLU459 3.1 29.8 1.0 C5 A:HZQ502 3.2 40.2 1.0 MN A:MN503 3.4 32.4 1.0 OE2 A:GLU459 3.4 28.0 1.0 OD2 A:ASP262 3.4 29.6 1.0 C10 A:HZQ502 3.6 38.3 1.0 CZ A:PHE219 3.7 20.9 1.0 CB A:ASP251 4.0 15.5 1.0 CE1 A:PHE219 4.0 24.3 1.0 NE2 A:GLN457 4.1 20.2 1.0 OE1 A:GLU364 4.2 36.3 1.0 CG A:GLU459 4.4 35.4 1.0 O A:HOH612 4.4 34.2 1.0 CB A:ASP262 4.4 25.1 1.0 O A:HOH725 4.4 37.4 1.0 C2 A:HZQ502 4.4 39.5 1.0 CB A:ALA264 4.5 17.2 1.0 N A:CYS263 4.5 21.6 1.0 C A:ASP262 4.6 25.8 1.0 CE2 A:PHE219 4.6 23.3 1.0 CA A:ASP262 4.7 23.7 1.0 CD A:GLU364 4.8 45.6 1.0 CA A:ASP251 4.8 13.9 1.0 OE2 A:GLU364 4.8 47.6 1.0 CB A:GLU459 4.8 24.9 1.0 N6 A:HZQ502 4.8 37.9 1.0 C A:CYS263 4.9 20.9 1.0 C7 A:HZQ502 4.9 38.0 1.0 O A:CYS263 5.0 18.1 1.0

T.Heinrich, J.Seenisamy, B.Blume, J.Bomke, M.Calderini, U.Eckert, M.Friese-Hamim, R.Kohl, M.Lehmann, B.Leuthner, D.Musil, F.Rohdich, F.T.Zenke. Discovery and Structure-Based Optimization of Next-Generation Reversible Methionine Aminopeptidase-2 (Metap-2) Inhibitors. J.Med.Chem. V. 62 5025 2019.
ISSN: ISSN 0022-2623
PubMed: 30939017
DOI: 10.1021/ACS.JMEDCHEM.9B00041