Chlorine 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:

Zinc

(Zn)

2 atoms

The binding sites of Chlorine 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 Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structure of Human Somatic Angiontensin-I Converting Enzyme N Domain with Lisinopril, PDB code: 2c6n:
Jump to Chlorine binding site number: 1; 2;

Chlorine 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 Chlorine with other atoms in the Cl 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:Cl703 b:31.9 occ:1.00 OH A:TYR202 2.9 28.6 1.0 NE A:ARG500 3.5 32.2 1.0 CB A:PRO497 3.6 22.3 1.0 CB A:ARG500 3.6 32.1 1.0 CG A:ARG500 3.6 33.1 1.0 CE1 A:TYR202 3.7 28.9 1.0 CZ A:TYR202 3.7 28.1 1.0 CG2 A:ILE499 3.8 28.2 1.0 CG A:PRO385 4.0 29.1 1.0 CB A:PRO385 4.0 28.9 1.0 N A:ARG500 4.2 29.7 1.0 CD A:ARG500 4.2 33.3 1.0 CE3 A:TRP201 4.3 50.0 1.0 CA A:ARG500 4.4 31.8 1.0 NH2 A:ARG500 4.4 30.8 1.0 CZ A:ARG500 4.5 31.2 1.0 CZ3 A:TRP201 4.5 51.1 1.0 O A:TRP198 4.6 32.4 1.0 CG A:PRO497 4.6 22.1 1.0 C A:ILE499 4.7 28.2 1.0 CA A:PRO497 4.8 22.4 1.0 C A:PRO497 4.8 22.2 1.0 N A:ILE499 4.9 24.4 1.0 CD1 A:TYR202 5.0 29.6 1.0

Chlorine 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 Chlorine with other atoms in the Cl 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:Cl702 b:25.0 occ:1.00 NE B:ARG500 3.0 30.8 1.0 OH B:TYR202 3.3 47.5 1.0 CB B:PRO497 3.3 28.1 1.0 CB B:PRO385 3.3 36.2 1.0 NH2 B:ARG500 3.4 26.8 1.0 CB B:ARG500 3.4 33.6 1.0 CZ B:ARG500 3.6 28.8 1.0 CG B:PRO385 3.7 37.0 1.0 CE3 B:TRP201 4.0 58.8 1.0 CG B:ARG500 4.0 33.3 1.0 N B:ARG500 4.0 33.6 1.0 CD B:ARG500 4.0 32.2 1.0 CG2 B:ILE499 4.1 32.7 1.0 CA B:ARG500 4.1 32.8 1.0 CZ3 B:TRP201 4.1 59.5 1.0 CZ B:TYR202 4.1 46.4 1.0 CE1 B:TYR202 4.2 45.9 1.0 CG B:PRO497 4.2 27.8 1.0 CA B:PRO497 4.6 28.5 1.0 C B:PRO497 4.7 28.7 1.0 CD B:PRO385 4.8 36.3 1.0 CA B:PRO385 4.8 36.6 1.0 C B:ILE499 4.9 33.2 1.0 NH1 B:ARG500 4.9 25.3 1.0 N B:TYR498 4.9 27.7 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