Chlorine in PDB 4c2p: Crystal Structure of Human Testis Angiotensin-I Converting Enzyme Mutant R522K in Complex with Captopril

All present enzymatic activity of Crystal Structure of Human Testis Angiotensin-I Converting Enzyme Mutant R522K in Complex with Captopril:
3.4.15.1;

The structure of Crystal Structure of Human Testis Angiotensin-I Converting Enzyme Mutant R522K in Complex with Captopril, PDB code: 4c2p was solved by G.Masuyer, C.J.Yates, S.L.U.Schwager, A.Mohd, 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)	44.74 / 1.99
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	57.140, 84.650, 135.180, 90.00, 90.00, 90.00
R / Rfree (%)	21.124 / 24.67

The structure of Crystal Structure of Human Testis Angiotensin-I Converting Enzyme Mutant R522K in Complex with Captopril also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Chlorine atom in the Crystal Structure of Human Testis Angiotensin-I Converting Enzyme Mutant R522K in Complex with Captopril (pdb code 4c2p). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Human Testis Angiotensin-I Converting Enzyme Mutant R522K in Complex with Captopril, PDB code: 4c2p:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Human Testis Angiotensin-I Converting Enzyme Mutant R522K in Complex with Captopril


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Human Testis Angiotensin-I Converting Enzyme Mutant R522K in Complex with Captopril within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl702 b:9.8 occ:1.00 NE A:ARG186 3.2 11.8 1.0 NE1 A:TRP485 3.3 10.6 1.0 NH1 A:ARG186 3.3 11.3 1.0 O A:HOH1057 3.4 9.1 1.0 NH1 A:ARG489 3.4 9.6 1.0 CZ2 A:TRP486 3.6 10.5 1.0 CZ A:ARG186 3.7 11.7 1.0 CB A:ASP507 3.7 10.6 1.0 NE A:ARG489 3.8 9.5 1.0 CZ A:ARG489 3.8 9.5 1.0 CH2 A:TRP486 4.0 10.3 1.0 CE2 A:TRP485 4.2 10.6 1.0 CD1 A:TRP485 4.2 10.9 1.0 CD A:ARG186 4.3 12.1 1.0 CE2 A:TRP486 4.3 10.6 1.0 CZ2 A:TRP485 4.4 10.4 1.0 O A:ASP507 4.4 10.5 1.0 CZ2 A:TRP182 4.4 10.3 1.0 CG A:ASP507 4.6 10.8 1.0 C A:ASP507 4.7 10.5 1.0 CA A:ASP507 4.8 10.7 1.0 NE1 A:TRP486 4.8 10.7 1.0 NH2 A:ARG489 4.9 9.2 1.0 CD A:ARG489 4.9 9.5 1.0 O A:HOH1004 4.9 7.2 1.0 OD2 A:ASP507 4.9 10.8 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Human Testis Angiotensin-I Converting Enzyme Mutant R522K in Complex with Captopril


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Human Testis Angiotensin-I Converting Enzyme Mutant R522K in Complex with Captopril within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl703 b:13.9 occ:1.00 OH A:TYR224 3.0 10.1 1.0 O A:HOH1045 3.1 13.3 1.0 O A:HOH1157 3.1 15.3 1.0 CB A:LYS522 3.5 10.3 1.0 CB A:PRO519 3.6 9.4 1.0 N A:LYS522 3.6 10.0 1.0 CG2 A:ILE521 3.7 9.7 1.0 CE1 A:TYR224 3.7 10.2 1.0 CZ A:TYR224 3.8 10.2 1.0 CG A:LYS522 3.8 10.4 1.0 CB A:PRO407 3.8 12.4 1.0 CG A:PRO407 3.9 12.6 1.0 CA A:LYS522 4.0 10.2 1.0 CD A:LYS522 4.2 10.6 1.0 C A:PRO519 4.5 9.4 1.0 N A:ILE521 4.5 9.6 1.0 C A:ILE521 4.5 9.8 1.0 O A:PRO519 4.6 9.4 1.0 CG A:PRO519 4.6 9.5 1.0 CA A:PRO519 4.7 9.4 1.0 O A:HOH1051 4.8 9.1 1.0 N A:TYR520 4.8 9.4 1.0 CA A:ILE521 4.8 9.7 1.0 CB A:ILE521 4.8 9.7 1.0 CD A:PRO407 4.9 12.6 1.0 CD1 A:TYR224 4.9 10.3 1.0

C.J.Yates, G.Masuyer, S.L.U.Schwager, A.Mohd, E.D.Sturrock, K.R.Acharya. Molecular and Thermodynamic Mechanisms of the Chloride Dependent Human Angiotensin-I Converting Enzyme (Ace) J.Biol.Chem. V. 289 1798 2014.
ISSN: ISSN 0021-9258
PubMed: 24297181
DOI: 10.1074/JBC.M113.512335