Zinc in PDB 2x8y: Crystal Structure of Ance

All present enzymatic activity of Crystal Structure of Ance:
3.4.15.1;

The structure of Crystal Structure of Ance, PDB code: 2x8y was solved by M.Akif, D.Georgiadis, A.Mahajan, V.Dive, E.D.Sturrock, R.E.Isaac, K.R.Acharya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.27 / 1.90
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	173.096, 173.096, 101.566, 90.00, 90.00, 120.00
R / Rfree (%)	19.4 / 22

The binding sites of Zinc atom in the Crystal Structure of Ance (pdb code 2x8y). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Ance, PDB code: 2x8y:

Zinc binding site 1 out of 1 in the Crystal Structure of Ance


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Ance within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn702 b:33.8 occ:1.00 OE1 A:GLU395 2.0 28.4 1.0 O A:HOH992 2.0 43.2 1.0 NE2 A:HIS371 2.0 29.7 1.0 NE2 A:HIS367 2.1 31.8 1.0 CD A:GLU395 3.0 28.0 1.0 CE1 A:HIS371 3.0 30.1 1.0 CE1 A:HIS367 3.0 31.6 1.0 CD2 A:HIS371 3.1 29.0 1.0 CD2 A:HIS367 3.1 31.4 1.0 OE2 A:GLU395 3.2 29.1 1.0 OHB A:FLC701 3.7 57.4 1.0 O A:HOH1194 3.7 38.6 1.0 ND1 A:HIS371 4.1 30.0 1.0 OH A:TYR507 4.1 29.3 1.0 CE1 A:TYR507 4.1 28.2 1.0 OB1 A:FLC701 4.1 56.1 1.0 ND1 A:HIS367 4.1 31.4 1.0 CG A:HIS371 4.2 29.6 1.0 CG A:HIS367 4.2 31.2 1.0 CG A:GLU395 4.3 28.5 1.0 OE2 A:GLU368 4.4 34.4 1.0 O A:HOH981 4.5 35.6 1.0 CA A:GLU395 4.6 28.9 1.0 OE1 A:GLU368 4.6 32.5 1.0 CZ A:TYR507 4.6 28.1 1.0 CB A:GLU395 4.7 28.8 1.0 CD A:GLU368 4.8 33.3 1.0 CB A:FLC701 4.9 56.4 1.0 CBC A:FLC701 4.9 56.7 1.0

M.Akif, D.Georgiadis, A.Mahajan, V.Dive, E.D.Sturrock, R.E.Isaac, K.R.Acharya. High Resolution Crystal Structures of Drosophila Melanogaster Angiotensin Converting Enzyme in Complex with Novel Inhibitors and Anti- Hypertensive Drugs. J.Mol.Biol. V. 400 502 2010.
ISSN: ISSN 0022-2836
PubMed: 20488190
DOI: 10.1016/J.JMB.2010.05.024