Chlorine in PDB 6tt1: Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with 33RE.

All present enzymatic activity of Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with 33RE.:
3.4.15.1;

The structure of Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with 33RE., PDB code: 6tt1 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)	44.59 / 1.80
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	73.166, 77.128, 82.867, 88.93, 64.53, 75.15
R / Rfree (%)	20 / 23.7

The structure of Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with 33RE. also contains other interesting chemical elements:

Zinc

(Zn)

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 33RE. (pdb code 6tt1). 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 33RE., PDB code: 6tt1:
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 33RE.


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 33RE. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl712 b:22.0 occ:1.00 HH A:TYR202 2.2 30.5 1.0 HE A:ARG500 2.4 36.0 1.0 HB3 A:ARG500 2.7 25.9 1.0 HH21 A:ARG500 2.8 37.2 1.0 HB2 A:PRO497 2.9 26.9 1.0 OH A:TYR202 3.0 25.4 1.0 HE2 A:TYR202 3.1 37.9 1.0 H A:ARG500 3.1 24.4 1.0 O A:HOH1058 3.1 25.2 1.0 HG2 A:PRO385 3.1 37.4 1.0 HG22 A:ILE499 3.1 26.8 1.0 HB2 A:PRO385 3.2 39.4 1.0 NE A:ARG500 3.3 30.0 1.0 HE3 A:TRP201 3.4 50.9 1.0 HG23 A:ILE499 3.4 26.8 1.0 NH2 A:ARG500 3.5 31.0 1.0 HZ3 A:TRP201 3.6 50.9 1.0 CB A:ARG500 3.6 21.6 1.0 N A:ARG500 3.7 20.3 1.0 CB A:PRO497 3.7 22.4 1.0 CG2 A:ILE499 3.7 22.3 1.0 CE2 A:TYR202 3.7 31.6 1.0 CZ A:TYR202 3.8 28.9 1.0 CB A:PRO385 3.8 32.8 1.0 HG2 A:PRO497 3.8 31.2 1.0 CG A:PRO385 3.9 31.2 1.0 HB3 A:PRO497 3.9 26.9 1.0 CZ A:ARG500 3.9 33.1 1.0 HG2 A:ARG500 3.9 28.7 1.0 HB3 A:PRO385 4.0 39.4 1.0 CE3 A:TRP201 4.1 42.4 1.0 CA A:ARG500 4.1 21.5 1.0 CG A:ARG500 4.1 23.9 1.0 HA A:ARG500 4.1 25.8 1.0 CZ3 A:TRP201 4.2 42.4 1.0 HG21 A:ILE499 4.2 26.8 1.0 H A:ILE499 4.2 26.7 1.0 HB2 A:ARG500 4.3 25.9 1.0 HH22 A:ARG500 4.3 37.2 1.0 CD A:ARG500 4.3 26.9 1.0 CG A:PRO497 4.3 26.0 1.0 HD2 A:PRO385 4.5 36.4 1.0 HG3 A:PRO385 4.5 37.4 1.0 N A:ILE499 4.6 22.2 1.0 C A:ILE499 4.7 21.1 1.0 CD A:PRO385 4.8 30.3 1.0 C A:PRO497 4.8 23.4 1.0 O A:HOH1041 4.9 21.9 1.0 CA A:PRO497 4.9 22.4 1.0 HD2 A:PRO497 4.9 30.3 1.0 N A:TYR498 4.9 21.5 1.0 H A:TYR498 4.9 25.8 1.0 HD3 A:ARG500 4.9 32.3 1.0 HD2 A:ARG500 4.9 32.3 1.0 CB A:ILE499 4.9 22.9 1.0 CA A:ILE499 5.0 21.9 1.0 CD2 A:TYR202 5.0 31.2 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 33RE.


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 33RE. within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl709 b:30.7 occ:1.00 HE B:ARG500 2.3 40.5 1.0 HH B:TYR202 2.3 37.9 1.0 HH21 B:ARG500 2.7 45.1 1.0 HB2 B:PRO497 2.8 36.4 1.0 HB3 B:ARG500 2.8 32.8 1.0 HE1 B:TYR202 3.0 43.9 1.0 O B:HOH946 3.0 36.1 1.0 NE B:ARG500 3.1 33.8 1.0 OH B:TYR202 3.2 31.6 1.0 H B:ARG500 3.2 30.4 1.0 HG2 B:PRO385 3.2 44.7 1.0 HG22 B:ILE499 3.2 30.8 1.0 HB2 B:PRO385 3.3 43.2 1.0 NH2 B:ARG500 3.4 37.5 1.0 HE3 B:TRP201 3.5 64.2 1.0 HG23 B:ILE499 3.6 30.8 1.0 CB B:PRO497 3.6 30.3 1.0 HG2 B:PRO497 3.7 38.3 1.0 CB B:ARG500 3.7 27.3 1.0 HZ3 B:TRP201 3.7 60.3 1.0 CZ B:ARG500 3.7 39.7 1.0 CE1 B:TYR202 3.7 36.6 1.0 HG2 B:ARG500 3.7 33.8 1.0 N B:ARG500 3.8 25.4 1.0 HB3 B:PRO497 3.8 36.4 1.0 CG2 B:ILE499 3.9 25.7 1.0 CB B:PRO385 3.9 36.0 1.0 CZ B:TYR202 3.9 33.5 1.0 CG B:PRO385 3.9 37.2 1.0 CG B:ARG500 4.0 28.1 1.0 HB3 B:PRO385 4.0 43.2 1.0 HH22 B:ARG500 4.2 45.1 1.0 CD B:ARG500 4.2 31.6 1.0 CE3 B:TRP201 4.2 53.5 1.0 CA B:ARG500 4.2 27.6 1.0 CG B:PRO497 4.2 31.9 1.0 H B:ILE499 4.2 30.5 1.0 HA B:ARG500 4.3 33.1 1.0 CZ3 B:TRP201 4.3 50.3 1.0 HG21 B:ILE499 4.4 30.8 1.0 HB2 B:ARG500 4.4 32.8 1.0 HD2 B:PRO385 4.5 49.2 1.0 N B:ILE499 4.6 25.4 1.0 HG3 B:PRO385 4.6 44.7 1.0 O B:HOH934 4.7 28.8 1.0 C B:ILE499 4.7 25.1 1.0 HD2 B:ARG500 4.7 37.9 1.0 HD3 B:ARG500 4.8 37.9 1.0 C B:PRO497 4.8 27.4 1.0 CD B:PRO385 4.8 41.0 1.0 HD2 B:PRO497 4.8 38.3 1.0 CA B:PRO497 4.9 26.8 1.0 HG3 B:PRO497 4.9 38.3 1.0 N B:TYR498 5.0 24.3 1.0 CD1 B:TYR202 5.0 40.8 1.0 HG3 B:ARG500 5.0 33.8 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