Chlorine in PDB 6tt3: Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6.

All present enzymatic activity of Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6.:
3.4.15.1;

The structure of Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6., PDB code: 6tt3 was solved by G.E.Cozier, K.R.Acharya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	75.11 / 1.70
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	73.617, 78.201, 83.789, 88.64, 64.35, 74.64
R / Rfree (%)	18.8 / 22.1

The structure of Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6. also contains other interesting chemical elements:

Zinc	(Zn)	2 atoms
Calcium	(Ca)	2 atoms

The binding sites of Chlorine atom in the Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6. (pdb code 6tt3). 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 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6., PDB code: 6tt3:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6.


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 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl713 b:17.9 occ:1.00 HH A:TYR202 2.3 21.5 1.0 HE A:ARG500 2.4 22.4 1.0 HH21 A:ARG500 2.7 23.7 1.0 HB3 A:ARG500 2.8 19.6 1.0 HB2 A:PRO497 3.0 20.1 1.0 H A:ARG500 3.1 19.2 1.0 HG22 A:ILE499 3.1 19.9 1.0 HE2 A:TYR202 3.1 21.9 1.0 OH A:TYR202 3.1 17.9 1.0 O A:HOH1074 3.2 20.5 1.0 NE A:ARG500 3.2 18.7 1.0 HB2 A:PRO385 3.2 22.2 1.0 HG2 A:PRO385 3.2 21.2 1.0 HZ3 A:TRP201 3.2 24.1 1.0 HE3 A:TRP201 3.3 26.4 1.0 NH2 A:ARG500 3.5 19.7 1.0 HG23 A:ILE499 3.6 19.9 1.0 CB A:ARG500 3.6 16.4 1.0 N A:ARG500 3.7 16.0 1.0 HB3 A:PRO497 3.8 20.1 1.0 CG2 A:ILE499 3.8 16.5 1.0 CZ A:ARG500 3.8 23.7 1.0 CB A:PRO497 3.8 16.7 1.0 CE2 A:TYR202 3.8 18.3 1.0 CB A:PRO385 3.8 18.5 1.0 HG2 A:ARG500 3.9 17.3 1.0 CZ3 A:TRP201 3.9 20.1 1.0 CZ A:TYR202 3.9 17.5 1.0 CE3 A:TRP201 3.9 22.0 1.0 CG A:PRO385 4.0 17.7 1.0 HB3 A:PRO385 4.0 22.2 1.0 CA A:ARG500 4.1 14.4 1.0 CG A:ARG500 4.1 14.4 1.0 HA A:ARG500 4.2 17.3 1.0 HH22 A:ARG500 4.2 23.7 1.0 CD A:ARG500 4.3 19.1 1.0 HG21 A:ILE499 4.3 19.9 1.0 HG2 A:PRO497 4.3 19.2 1.0 H A:ILE499 4.3 21.3 1.0 HB2 A:ARG500 4.4 19.6 1.0 HD2 A:PRO385 4.5 22.7 1.0 HG3 A:PRO385 4.6 21.2 1.0 CG A:PRO497 4.7 16.0 1.0 N A:ILE499 4.7 17.8 1.0 C A:ILE499 4.7 17.1 1.0 CD A:PRO385 4.8 18.9 1.0 HD2 A:ARG500 4.8 22.9 1.0 O A:HOH999 4.8 17.3 1.0 HD3 A:ARG500 4.8 22.9 1.0 C A:PRO497 4.9 24.3 1.0 CA A:PRO497 5.0 17.5 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6.


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 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6. within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl709 b:26.5 occ:1.00 HE B:ARG500 2.3 30.7 1.0 HH B:TYR202 2.4 34.0 1.0 HB3 B:ARG500 2.7 21.3 1.0 HH21 B:ARG500 2.8 37.0 1.0 HB2 B:PRO497 3.0 26.4 1.0 HE1 B:TYR202 3.1 39.6 1.0 HG22 B:ILE499 3.1 28.9 1.0 H B:ARG500 3.1 27.1 1.0 NE B:ARG500 3.1 25.6 1.0 O B:HOH992 3.1 28.9 1.0 HB2 B:PRO385 3.2 39.7 1.0 HG2 B:PRO385 3.2 38.1 1.0 OH B:TYR202 3.3 28.3 1.0 HE3 B:TRP201 3.4 41.8 1.0 HZ3 B:TRP201 3.4 36.8 1.0 NH2 B:ARG500 3.5 30.8 1.0 CB B:ARG500 3.6 17.7 1.0 HB3 B:PRO497 3.6 26.4 1.0 HG23 B:ILE499 3.7 28.9 1.0 CB B:PRO497 3.7 22.0 1.0 HG2 B:ARG500 3.7 23.6 1.0 N B:ARG500 3.7 22.5 1.0 CZ B:ARG500 3.8 34.7 1.0 CE1 B:TYR202 3.8 33.0 1.0 CG2 B:ILE499 3.8 24.1 1.0 CB B:PRO385 3.8 33.1 1.0 HB3 B:PRO385 3.9 39.7 1.0 CG B:PRO385 4.0 31.8 1.0 CZ B:TYR202 4.0 35.9 1.0 CG B:ARG500 4.0 19.6 1.0 CE3 B:TRP201 4.0 34.8 1.0 CZ3 B:TRP201 4.0 30.6 1.0 CA B:ARG500 4.1 20.9 1.0 CD B:ARG500 4.2 27.8 1.0 HG2 B:PRO497 4.2 25.3 1.0 HA B:ARG500 4.2 25.0 1.0 HG21 B:ILE499 4.2 28.9 1.0 HH22 B:ARG500 4.2 37.0 1.0 HB2 B:ARG500 4.3 21.3 1.0 H B:ILE499 4.4 23.6 1.0 CG B:PRO497 4.6 21.1 1.0 HD2 B:PRO385 4.6 43.8 1.0 HG3 B:PRO385 4.6 38.1 1.0 C B:ILE499 4.7 22.1 1.0 N B:ILE499 4.7 19.6 1.0 HD2 B:ARG500 4.7 33.4 1.0 HD3 B:ARG500 4.8 33.4 1.0 O B:HOH942 4.8 26.8 1.0 C B:PRO497 4.9 27.6 1.0 CD B:PRO385 4.9 36.4 1.0 CA B:PRO497 4.9 21.1 1.0 HG3 B:ARG500 5.0 23.6 1.0

G.E.Cozier, L.Lubbe, E.D.Sturrock, K.R.Acharya. Ace-Domain Selectivity Extends Beyond Direct Interacting Residues at the Active Site. Biochem.J. 2020.
ISSN: ESSN 1470-8728
PubMed: 32195541
DOI: 10.1042/BCJ20200060