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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 6qeh:

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:

Manganese (Mn) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine 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 Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Human Methionine Aminopeptidase-2 in Complex with An Inhibitor 5-Chloro-Quinolin-8-Ol, PDB code: 6qeh:

Chlorine binding site 1 out of 1 in 6qeh

Go back to Chlorine Binding Sites List in 6qeh
Chlorine binding site 1 out of 1 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 Chlorine with other atoms in the Cl 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:Cl502

b:39.4
occ:1.00
CL8 A:HZQ502 0.0 39.4 1.0
C3 A:HZQ502 1.7 38.8 1.0
C7 A:HZQ502 2.7 38.0 1.0
C1 A:HZQ502 2.7 39.1 1.0
C4 A:HZQ502 3.1 35.5 1.0
NE2 A:HIS231 3.7 27.7 1.0
CD2 A:HIS231 4.0 27.3 1.0
CD2 A:HIS382 4.0 17.3 1.0
C10 A:HZQ502 4.0 38.3 1.0
C2 A:HZQ502 4.1 39.5 1.0
CE1 A:HIS231 4.3 27.3 1.0
CB A:ALA414 4.4 16.9 1.0
C9 A:HZQ502 4.4 36.0 1.0
C5 A:HZQ502 4.5 40.2 1.0
CG A:HIS231 4.6 25.1 1.0
CB A:TYR444 4.6 23.5 1.0
CG A:TYR444 4.6 26.3 1.0
CD1 A:TYR444 4.7 29.2 1.0
CG A:HIS382 4.7 16.8 1.0
ND1 A:HIS231 4.7 27.1 1.0
CB A:HIS382 4.8 14.3 1.0

Reference:

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
Page generated: Sat Jul 12 18:53:32 2025

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