Chlorine in PDB 6zpu: Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus.

All present enzymatic activity of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus.:
3.4.15.1;

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus., PDB code: 6zpu 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)	53.18 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.453, 84.904, 128.154, 90.00, 90.00, 90.00
R / Rfree (%)	19.1 / 23.5

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus. also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Chlorine atom in the Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus. (pdb code 6zpu). 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 Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus., PDB code: 6zpu:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus.


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 Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl717 b:24.6 occ:1.00 HH A:TYR224 2.3 33.9 1.0 HE A:ARG522 2.4 19.8 1.0 HB3 A:ARG522 2.7 21.2 1.0 HB2 A:PRO519 2.8 26.3 1.0 HG22 A:ILE521 2.9 24.9 1.0 HE1 A:TYR224 2.9 27.0 1.0 HH21 A:ARG522 3.0 24.7 1.0 O A:HOH1026 3.0 28.1 1.0 H A:ARG522 3.1 25.9 1.0 OH A:TYR224 3.1 28.2 1.0 HB2 A:PRO407 3.1 27.4 1.0 HG2 A:PRO407 3.2 29.3 1.0 NE A:ARG522 3.2 16.5 1.0 CB A:ARG522 3.5 17.7 1.0 CE1 A:TYR224 3.6 22.5 1.0 CB A:PRO519 3.6 21.9 1.0 HB3 A:PRO519 3.6 26.3 1.0 N A:ARG522 3.6 21.6 1.0 NH2 A:ARG522 3.7 20.6 1.0 CG2 A:ILE521 3.7 20.8 1.0 HG2 A:ARG522 3.7 22.5 1.0 HG23 A:ILE521 3.7 24.9 1.0 CZ A:TYR224 3.8 21.6 1.0 CB A:PRO407 3.8 22.9 1.0 HB3 A:PRO407 3.8 27.4 1.0 CG A:PRO407 3.9 24.4 1.0 CZ A:ARG522 3.9 23.4 1.0 CA A:ARG522 4.0 19.3 1.0 CG A:ARG522 4.0 18.8 1.0 HA A:ARG522 4.0 23.1 1.0 HG21 A:ILE521 4.1 24.9 1.0 HG2 A:PRO519 4.1 33.2 1.0 CD A:ARG522 4.2 19.8 1.0 HB2 A:ARG522 4.2 21.2 1.0 H A:ILE521 4.4 27.7 1.0 CG A:PRO519 4.4 27.6 1.0 SD A:MET223 4.4 31.5 1.0 HH22 A:ARG522 4.5 24.7 1.0 HG3 A:PRO407 4.5 29.3 1.0 HB2 A:MET223 4.6 23.8 1.0 C A:ILE521 4.6 24.3 1.0 C A:PRO519 4.7 26.1 1.0 N A:ILE521 4.7 23.1 1.0 HD2 A:PRO407 4.7 28.0 1.0 CA A:PRO519 4.8 23.2 1.0 HD3 A:ARG522 4.8 23.7 1.0 CD1 A:TYR224 4.8 27.0 1.0 O A:PRO519 4.8 20.6 1.0 HD2 A:ARG522 4.8 23.7 1.0 O A:HOH895 4.9 20.8 1.0 CD A:PRO407 4.9 23.4 1.0 N A:TYR520 4.9 22.2 1.0 CB A:ILE521 4.9 22.6 1.0 HG3 A:ARG522 4.9 22.5 1.0 HB3 A:TRP220 5.0 28.6 1.0 CA A:ILE521 5.0 23.3 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus.


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 Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl718 b:28.3 occ:1.00 HH11 A:ARG186 2.2 29.2 1.0 HE A:ARG186 2.3 30.4 1.0 HE1 A:TRP485 2.6 31.7 1.0 HH11 A:ARG489 2.7 32.0 1.0 HB3 A:ASP507 2.9 32.4 1.0 NH1 A:ARG186 3.0 24.4 1.0 NE A:ARG186 3.1 25.3 1.0 O A:HOH860 3.2 27.2 1.0 NH1 A:ARG489 3.2 26.7 1.0 HZ2 A:TRP486 3.3 32.1 1.0 HE A:ARG489 3.4 22.4 1.0 NE1 A:TRP485 3.5 26.4 1.0 CZ A:ARG186 3.5 18.3 1.0 CZ2 A:TRP486 3.6 26.8 1.0 HH12 A:ARG489 3.6 32.0 1.0 HH12 A:ARG186 3.7 29.2 1.0 HZ2 A:TRP485 3.8 33.2 1.0 CB A:ASP507 3.8 27.0 1.0 HZ2 A:TRP182 3.8 22.7 1.0 CZ A:ARG489 3.8 21.9 1.0 NE A:ARG489 3.8 18.7 1.0 HH2 A:TRP486 3.9 33.7 1.0 HB2 A:ASP507 4.0 32.4 1.0 CH2 A:TRP486 4.0 28.1 1.0 HD1 A:TRP279 4.2 27.4 1.0 CE2 A:TRP485 4.3 26.3 1.0 HD3 A:ARG186 4.3 33.5 1.0 CD A:ARG186 4.3 27.9 1.0 CZ2 A:TRP485 4.4 27.6 1.0 CE2 A:TRP486 4.4 28.8 1.0 CZ2 A:TRP182 4.4 18.9 1.0 HE1 A:TRP182 4.5 25.5 1.0 O A:ASP507 4.5 24.3 1.0 CD1 A:TRP485 4.5 27.6 1.0 CG A:ASP507 4.5 27.0 1.0 HD1 A:TRP485 4.6 33.1 1.0 HG2 A:ARG186 4.7 33.0 1.0 C A:ASP507 4.8 25.4 1.0 HA A:TRP279 4.8 25.0 1.0 CA A:ASP507 4.8 25.2 1.0 HE1 A:TRP486 4.8 37.0 1.0 NH2 A:ARG186 4.8 25.2 1.0 O A:HOH919 4.9 23.3 1.0 NH2 A:ARG489 4.9 18.0 1.0 OD2 A:ASP507 4.9 26.2 1.0 HG3 A:ARG489 4.9 31.9 1.0 NE1 A:TRP182 4.9 21.2 1.0 NE1 A:TRP486 4.9 30.8 1.0 HD3 A:ARG489 5.0 21.0 1.0 CD A:ARG489 5.0 17.5 1.0 HA A:ASP507 5.0 30.3 1.0 CE2 A:TRP182 5.0 18.2 1.0 CZ3 A:TRP486 5.0 24.1 1.0

G.E.Cozier, L.Lubbe, E.D.Sturrock, K.R.Acharya. Angiotensin-Converting Enzyme Open For Business: Structural Insights Into the Sub-Domain Dynamics. Febs J. 2020.
ISSN: ISSN 1742-464X
PubMed: 33067882
DOI: 10.1111/FEBS.15601