Zinc in PDB 3qz2: The Structure of Cysteine-Free Human Insulin Degrading Enzyme

All present enzymatic activity of The Structure of Cysteine-Free Human Insulin Degrading Enzyme:
3.4.24.56;

The structure of The Structure of Cysteine-Free Human Insulin Degrading Enzyme, PDB code: 3qz2 was solved by Q.Guo, W.J.Tang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 3.20
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	262.073, 262.073, 90.838, 90.00, 90.00, 120.00
R / Rfree (%)	17.2 / 24.1

The binding sites of Zinc atom in the The Structure of Cysteine-Free Human Insulin Degrading Enzyme (pdb code 3qz2). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the The Structure of Cysteine-Free Human Insulin Degrading Enzyme, PDB code: 3qz2:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the The Structure of Cysteine-Free Human Insulin Degrading Enzyme


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Structure of Cysteine-Free Human Insulin Degrading Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1 b:27.9 occ:1.00 OE1 A:GLU189 2.1 19.0 1.0 NE2 A:HIS112 2.1 24.6 1.0 NE2 A:HIS108 2.3 14.2 1.0 OE2 A:GLU189 2.4 20.4 1.0 CD A:GLU189 2.6 20.3 1.0 CE1 A:HIS112 3.0 24.4 1.0 CD2 A:HIS112 3.1 23.3 1.0 CD2 A:HIS108 3.3 17.4 1.0 CE1 A:HIS108 3.3 15.8 1.0 CG A:GLU189 4.1 18.9 1.0 ND1 A:HIS112 4.1 22.4 1.0 OH A:TYR831 4.1 27.6 1.0 OE1 A:GLU111 4.2 23.9 1.0 CG A:HIS112 4.2 20.8 1.0 OE2 A:GLU111 4.3 23.2 1.0 CE1 A:TYR831 4.3 25.3 1.0 ND1 A:HIS108 4.4 17.7 1.0 CG A:HIS108 4.5 18.6 1.0 CD A:GLU111 4.7 21.6 1.0 CZ A:TYR831 4.7 25.8 1.0 CB A:GLU189 4.9 20.2 1.0

Zinc binding site 2 out of 2 in the The Structure of Cysteine-Free Human Insulin Degrading Enzyme


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Structure of Cysteine-Free Human Insulin Degrading Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn2 b:28.8 occ:1.00 OE1 B:GLU189 2.1 24.3 1.0 NE2 B:HIS112 2.1 27.1 1.0 NE2 B:HIS108 2.2 17.5 1.0 OE2 B:GLU189 2.7 25.8 1.0 CD B:GLU189 2.7 23.7 1.0 CD2 B:HIS112 2.9 27.0 1.0 CE1 B:HIS108 3.0 17.6 1.0 CE1 B:HIS112 3.2 28.3 1.0 CD2 B:HIS108 3.3 18.8 1.0 CG B:HIS112 4.1 24.9 1.0 ND1 B:HIS112 4.2 26.6 1.0 ND1 B:HIS108 4.2 18.1 1.0 CG B:GLU189 4.3 22.4 1.0 OE1 B:GLU111 4.3 23.9 1.0 OH B:TYR831 4.3 33.3 1.0 CG B:HIS108 4.3 17.0 1.0 OE2 B:GLU111 4.4 24.9 1.0 CE1 B:TYR831 4.5 31.6 1.0 CD B:GLU111 4.7 23.6 1.0 CZ B:TYR831 4.7 30.9 1.0 CB B:GLU189 4.9 22.6 1.0

J.Charton, M.Gauriot, Q.Guo, N.Hennuyer, X.Marechal, J.Dumont, M.Hamdane, V.Pottiez, V.Landry, O.Sperandio, M.Flipo, L.Buee, B.Staels, F.Leroux, W.J.Tang, B.Deprez, R.Deprez-Poulain. Imidazole-Derived 2-[N-Carbamoylmethyl-Alkylamino]Acetic Acids, Substrate-Dependent Modulators of Insulin-Degrading Enzyme in Amyloid-Beta Hydrolysis. Eur.J.Med.Chem. V. 79 184 2014.
ISSN: ISSN 0223-5234
PubMed: 24735644
DOI: 10.1016/J.EJMECH.2014.04.009