Zinc in PDB 4bzs: Human Angiotenisn Converting Enzyme N-Domain in Complex with K-26

All present enzymatic activity of Human Angiotenisn Converting Enzyme N-Domain in Complex with K-26:
3.4.15.1;

The structure of Human Angiotenisn Converting Enzyme N-Domain in Complex with K-26, PDB code: 4bzs was solved by G.J.Kramer, A.Mohd, S.L.U.Schwager, G.Masuyer, K.R.Acharya, E.D.Sturrock, B.O.Bachmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.61 / 2.10
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	73.005, 77.320, 82.070, 88.69, 64.53, 75.29
R / Rfree (%)	23.314 / 27.681

The structure of Human Angiotenisn Converting Enzyme N-Domain in Complex with K-26 also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Zinc atom in the Human Angiotenisn Converting Enzyme N-Domain in Complex with K-26 (pdb code 4bzs). 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 Angiotenisn Converting Enzyme N-Domain in Complex with K-26, PDB code: 4bzs:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Human Angiotenisn Converting Enzyme N-Domain in Complex with K-26


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Angiotenisn Converting Enzyme N-Domain in Complex with K-26 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn701 b:35.5 occ:1.00 OE1 A:GLU389 1.9 28.3 1.0 OAK A:K261001 2.1 27.8 1.0 NE2 A:HIS365 2.2 25.6 1.0 NE2 A:HIS361 2.2 28.4 1.0 OAG A:K261001 2.5 25.4 1.0 PBK A:K261001 2.7 27.1 1.0 CE1 A:HIS365 2.8 25.8 1.0 CE1 A:HIS361 2.9 28.3 1.0 CD A:GLU389 3.0 29.6 1.0 CD2 A:HIS361 3.3 28.6 1.0 OE2 A:GLU389 3.4 29.2 1.0 CD2 A:HIS365 3.4 26.0 1.0 OAJ A:K261001 3.8 27.9 1.0 ND1 A:HIS361 4.0 28.5 1.0 CE1 A:TYR501 4.0 26.1 1.0 ND1 A:HIS365 4.1 26.3 1.0 OH A:TYR501 4.1 26.1 1.0 NAY A:K261001 4.2 28.5 1.0 CBI A:K261001 4.2 27.9 1.0 O A:HOH2044 4.2 25.9 1.0 CG A:GLU389 4.3 30.0 1.0 CG A:HIS361 4.3 28.3 1.0 CG A:HIS365 4.4 26.6 1.0 CA A:GLU389 4.4 31.1 1.0 CB A:GLU389 4.5 30.5 1.0 CZ A:TYR501 4.6 25.9 1.0 C A:K261001 4.8 29.3 1.0 CB A:K261001 4.9 30.9 1.0 OE2 A:GLU362 5.0 33.2 1.0

Zinc binding site 2 out of 2 in the Human Angiotenisn Converting Enzyme N-Domain in Complex with K-26


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human Angiotenisn Converting Enzyme N-Domain in Complex with K-26 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn701 b:37.0 occ:1.00 OAK B:K261001 2.0 26.5 1.0 OE1 B:GLU389 2.1 31.2 1.0 NE2 B:HIS365 2.1 23.8 1.0 OAG B:K261001 2.3 26.9 1.0 NE2 B:HIS361 2.4 28.6 1.0 PBK B:K261001 2.6 26.6 1.0 CE1 B:HIS365 2.9 24.0 1.0 CD B:GLU389 3.0 31.5 1.0 CD2 B:HIS365 3.2 24.0 1.0 OE2 B:GLU389 3.3 32.4 1.0 CE1 B:HIS361 3.3 28.7 1.0 CD2 B:HIS361 3.3 28.6 1.0 NAY B:K261001 3.7 28.6 1.0 OAJ B:K261001 3.8 27.3 1.0 CBI B:K261001 3.8 27.9 1.0 CE1 B:TYR501 4.1 24.8 1.0 OH B:TYR501 4.1 25.2 1.0 ND1 B:HIS365 4.1 24.2 1.0 O B:HOH2064 4.1 26.6 1.0 CG B:HIS365 4.3 24.3 1.0 ND1 B:HIS361 4.3 28.4 1.0 CG B:HIS361 4.4 28.0 1.0 CG B:GLU389 4.4 31.0 1.0 C B:K261001 4.5 29.5 1.0 CB B:K261001 4.5 31.3 1.0 CZ B:TYR501 4.6 25.0 1.0 CA B:GLU389 4.8 30.5 1.0 OE2 B:GLU362 4.8 32.3 1.0 CB B:GLU389 4.8 30.7 1.0 CAV B:K261001 4.9 29.1 1.0 OE1 B:GLU362 5.0 32.5 1.0

G.J.Kramer, A.Mohd, S.L.U.Schwager, G.Masuyer, K.R.Acharya, E.D.Sturrock, B.O.Bachmann. Interkingdom Pharmacology of Angiotensin-I Converting Enzyme Inhibitor Phosphonates Produced By Actinomycetes Acs Med.Chem.Lett. V. 5 346 2014.
ISSN: ISSN 1948-5875
PubMed: 24900839
DOI: 10.1021/ML4004588