Zinc in PDB 2c6n: Structure of Human Somatic Angiontensin-I Converting Enzyme N Domain with Lisinopril

All present enzymatic activity of Structure of Human Somatic Angiontensin-I Converting Enzyme N Domain with Lisinopril:
3.4.15.1;

The structure of Structure of Human Somatic Angiontensin-I Converting Enzyme N Domain with Lisinopril, PDB code: 2c6n was solved by H.R.Corradi, S.L.U.Schwager, A.Nichinda, E.D.Sturrock, K.R.Acharya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.76 / 3.00
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	101.300, 210.900, 171.000, 90.00, 90.00, 90.00
R / Rfree (%)	29.4 / 30.8

The structure of Structure of Human Somatic Angiontensin-I Converting Enzyme N Domain with Lisinopril also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Zinc atom in the Structure of Human Somatic Angiontensin-I Converting Enzyme N Domain with Lisinopril (pdb code 2c6n). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Human Somatic Angiontensin-I Converting Enzyme N Domain with Lisinopril, PDB code: 2c6n:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of Human Somatic Angiontensin-I Converting Enzyme N Domain with Lisinopril


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Human Somatic Angiontensin-I Converting Enzyme N Domain with Lisinopril within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn701 b:33.6 occ:1.00 OE1 A:GLU389 1.8 26.6 1.0 NE2 A:HIS361 2.0 29.9 1.0 NE2 A:HIS365 2.2 34.6 1.0 O3 A:LPR705 2.5 49.8 1.0 O2 A:LPR705 2.6 49.4 1.0 CE1 A:HIS361 2.6 30.8 1.0 CD A:GLU389 2.9 28.4 1.0 C3 A:LPR705 2.9 49.7 1.0 CE1 A:HIS365 3.1 34.4 1.0 CD2 A:HIS365 3.2 35.0 1.0 CD2 A:HIS361 3.2 30.4 1.0 OE2 A:GLU389 3.3 27.3 1.0 ND1 A:HIS361 3.8 32.8 1.0 CG A:HIS361 4.1 31.7 1.0 CG A:GLU389 4.2 29.2 1.0 ND1 A:HIS365 4.2 35.3 1.0 CE2 A:TYR501 4.2 46.5 1.0 CG A:HIS365 4.3 35.7 1.0 OH A:TYR501 4.3 46.1 1.0 C4 A:LPR705 4.4 48.7 1.0 CA A:GLU389 4.4 32.0 1.0 CB A:GLU389 4.5 31.3 1.0 OE2 A:GLU362 4.6 37.5 1.0 C2 A:LPR705 4.8 47.4 1.0 CZ A:TYR501 4.8 46.1 1.0 O A:HOH2001 4.8 1.8 1.0 N1 A:LPR705 4.8 47.8 1.0 OE1 A:GLU362 4.9 40.0 1.0

Zinc binding site 2 out of 2 in the Structure of Human Somatic Angiontensin-I Converting Enzyme N Domain with Lisinopril


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Human Somatic Angiontensin-I Converting Enzyme N Domain with Lisinopril within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn701 b:31.3 occ:1.00 OE1 B:GLU389 1.7 39.0 1.0 NE2 B:HIS361 2.0 31.9 1.0 O2 B:LPR705 2.0 36.9 1.0 O3 B:LPR705 2.0 38.6 1.0 NE2 B:HIS365 2.2 37.8 1.0 C3 B:LPR705 2.3 38.8 1.0 CE1 B:HIS361 2.5 32.6 1.0 CD B:GLU389 2.9 40.9 1.0 CE1 B:HIS365 3.2 35.7 1.0 CD2 B:HIS365 3.2 36.9 1.0 CD2 B:HIS361 3.2 32.9 1.0 OE2 B:GLU389 3.6 40.0 1.0 ND1 B:HIS361 3.7 33.3 1.0 C4 B:LPR705 3.8 38.9 1.0 CG B:GLU389 4.0 42.9 1.0 CG B:HIS361 4.1 34.4 1.0 CA B:GLU389 4.2 41.9 1.0 N1 B:LPR705 4.2 38.6 1.0 CB B:GLU389 4.2 43.1 1.0 ND1 B:HIS365 4.3 34.4 1.0 C2 B:LPR705 4.3 39.0 1.0 CG B:HIS365 4.3 36.2 1.0 C14 B:LPR705 4.5 39.8 1.0 CE2 B:TYR501 4.7 42.6 1.0 OE1 B:GLU362 4.7 45.6 1.0 OH B:TYR501 4.9 44.5 1.0 C8 B:LPR705 4.9 43.7 1.0 N B:GLU389 4.9 40.3 1.0

H.R.Corradi, S.L.Schwager, A.T.Nchinda, E.D.Sturrock, K.R.Acharya. Crystal Structure of the N Domain of Human Somatic Angiotensin I-Converting Enzyme Provides A Structural Basis For Domain-Specific Inhibitor Design. J. Mol. Biol. V. 357 964 2006.
ISSN: ISSN 0022-2836
PubMed: 16476442
DOI: 10.1016/J.JMB.2006.01.048