Zinc in PDB 4ca6: Human Angiotensin Converting Enzyme N-Domain in Complex with A Phosphinic Tripeptide Fi

All present enzymatic activity of Human Angiotensin Converting Enzyme N-Domain in Complex with A Phosphinic Tripeptide Fi:
3.4.15.1;

The structure of Human Angiotensin Converting Enzyme N-Domain in Complex with A Phosphinic Tripeptide Fi, PDB code: 4ca6 was solved by G.Masuyer, M.Akif, B.Czarny, F.Beau, S.L.U.Schwager, E.D.Sturrock, R.E.Isaac, V.Dive, K.R.Acharya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.74 / 1.91
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	72.925, 76.643, 82.545, 88.62, 64.22, 75.58
R / Rfree (%)	18.675 / 22.296

The structure of Human Angiotensin Converting Enzyme N-Domain in Complex with A Phosphinic Tripeptide Fi also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Zinc atom in the Human Angiotensin Converting Enzyme N-Domain in Complex with A Phosphinic Tripeptide Fi (pdb code 4ca6). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Human Angiotensin Converting Enzyme N-Domain in Complex with A Phosphinic Tripeptide Fi, PDB code: 4ca6:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Human Angiotensin Converting Enzyme N-Domain in Complex with A Phosphinic Tripeptide Fi


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Angiotensin Converting Enzyme N-Domain in Complex with A Phosphinic Tripeptide Fi within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1001 b:18.1 occ:1.00 NE2 A:HIS361 2.0 15.5 1.0 OE1 A:GLU389 2.0 20.0 1.0 NE2 A:HIS365 2.1 17.4 1.0 OAD A:3EF1630 2.1 19.4 1.0 OAG A:3EF1630 2.5 19.7 1.0 PBY A:3EF1630 2.7 20.6 1.0 CD A:GLU389 2.9 19.4 1.0 CE1 A:HIS361 2.9 15.3 1.0 CE1 A:HIS365 3.0 18.1 1.0 CD2 A:HIS361 3.0 15.5 1.0 OE2 A:GLU389 3.0 18.9 1.0 CD2 A:HIS365 3.1 17.8 1.0 NBI A:3EF1630 3.9 21.2 1.0 ND1 A:HIS361 4.0 15.4 1.0 CBX A:3EF1630 4.1 20.1 1.0 CG A:HIS361 4.1 15.4 1.0 CBF A:3EF1630 4.1 20.2 1.0 CE1 A:TYR501 4.1 15.8 1.0 ND1 A:HIS365 4.1 17.7 1.0 CG A:HIS365 4.2 17.3 1.0 CBM A:3EF1630 4.2 23.9 1.0 CBV A:3EF1630 4.2 21.1 1.0 CG A:GLU389 4.3 18.9 1.0 OH A:TYR501 4.3 16.6 1.0 O A:HOH2237 4.4 23.6 1.0 CA A:GLU389 4.6 18.7 1.0 OBJ A:3EF1630 4.7 24.6 1.0 OAB A:3EF1630 4.7 22.3 1.0 CB A:GLU389 4.7 18.8 1.0 OE1 A:GLU362 4.7 17.9 1.0 CZ A:TYR501 4.8 15.8 1.0 CBN A:3EF1630 4.8 21.1 1.0 OE2 A:GLU362 4.9 17.8 1.0

Zinc binding site 2 out of 2 in the Human Angiotensin Converting Enzyme N-Domain in Complex with A Phosphinic Tripeptide Fi


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human Angiotensin Converting Enzyme N-Domain in Complex with A Phosphinic Tripeptide Fi within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1001 b:16.6 occ:1.00 OE1 B:GLU389 1.9 14.1 1.0 NE2 B:HIS365 2.0 17.3 1.0 NE2 B:HIS361 2.0 15.0 1.0 OAD B:3EF1630 2.2 21.1 1.0 OAG B:3EF1630 2.4 18.3 1.0 PBY B:3EF1630 2.7 20.1 1.0 CD B:GLU389 2.8 14.8 1.0 CE1 B:HIS365 2.9 18.0 1.0 CE1 B:HIS361 2.9 15.2 1.0 CD2 B:HIS361 3.0 14.5 1.0 CD2 B:HIS365 3.1 17.6 1.0 OE2 B:GLU389 3.1 14.6 1.0 NBI B:3EF1630 3.9 20.9 1.0 ND1 B:HIS361 4.0 14.9 1.0 CBX B:3EF1630 4.0 20.1 1.0 ND1 B:HIS365 4.0 18.1 1.0 CG B:HIS361 4.1 14.7 1.0 CE1 B:TYR501 4.1 17.1 1.0 CBF B:3EF1630 4.1 20.2 1.0 CG B:HIS365 4.2 18.0 1.0 CBM B:3EF1630 4.2 23.0 1.0 CG B:GLU389 4.2 15.1 1.0 OH B:TYR501 4.3 17.4 1.0 CBV B:3EF1630 4.3 20.4 1.0 O B:HOH2191 4.3 18.9 1.0 CA B:GLU389 4.5 17.0 1.0 CB B:GLU389 4.6 16.2 1.0 OAB B:3EF1630 4.6 20.0 1.0 OBJ B:3EF1630 4.7 24.6 1.0 CZ B:TYR501 4.7 17.1 1.0 OE1 B:GLU362 4.7 17.5 1.0 OE2 B:GLU362 4.8 17.7 1.0 CBN B:3EF1630 4.9 19.4 1.0 CBB B:3EF1630 5.0 26.0 1.0

G.Masuyer, M.Akif, B.Czarny, F.Beau, S.L.Schwager, E.D.Sturrock, R.E.Isaac, V.Dive, K.R.Acharya. Crystal Structures of Highly Specific Phosphinic Tripeptide Enantiomers in Complex with the Angiotensin-I Converting Enzyme. Febs J. V. 281 943 2014.
ISSN: ISSN 1742-464X
PubMed: 24289879
DOI: 10.1111/FEBS.12660