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Chlorine in PDB 7q27: Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD011

Enzymatic activity of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD011

All present enzymatic activity of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD011:
3.4.15.1;

Protein crystallography data

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD011, PDB code: 7q27 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) 47.13 / 1.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.454, 85.586, 134.052, 90, 90, 90
R / Rfree (%) 14.9 / 17.8

Other elements in 7q27:

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD011 also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD011 (pdb code 7q27). 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 in Complex with Dual Ace/Nep Inhibitor AD011, PDB code: 7q27:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 7q27

Go back to Chlorine Binding Sites List in 7q27
Chlorine binding site 1 out of 2 in the Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD011


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 in Complex with Dual Ace/Nep Inhibitor AD011 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl708

b:12.9
occ:1.00
HE A:ARG186 2.4 11.0 1.0
HH21 A:ARG186 2.5 12.0 1.0
HE1 A:TRP485 2.5 12.3 1.0
HH21 A:ARG489 2.8 13.2 1.0
HB3 A:ASP507 2.9 10.9 1.0
HZ2 A:TRP486 3.1 12.0 1.0
NE A:ARG186 3.2 9.2 1.0
NH2 A:ARG186 3.2 10.0 1.0
NH2 A:ARG489 3.3 11.0 1.0
O A:HOH1042 3.3 16.9 1.0
NE1 A:TRP485 3.3 10.2 1.0
CZ2 A:TRP486 3.6 10.0 1.0
HE A:ARG489 3.6 10.7 1.0
HH22 A:ARG489 3.7 13.2 1.0
CZ A:ARG186 3.7 10.0 1.0
HZ2 A:TRP182 3.8 8.6 1.0
CB A:ASP507 3.8 9.1 1.0
HZ2 A:TRP485 3.9 11.9 1.0
CZ A:ARG489 3.9 9.6 1.0
NE A:ARG489 3.9 8.9 1.0
HH22 A:ARG186 4.0 12.0 1.0
HB2 A:ASP507 4.0 10.9 1.0
HH2 A:TRP486 4.0 11.8 1.0
CH2 A:TRP486 4.1 9.9 1.0
CE2 A:TRP485 4.2 8.9 1.0
HD3 A:ARG186 4.2 14.2 1.0
CD A:ARG186 4.3 11.9 1.0
CD1 A:TRP485 4.3 10.1 1.0
HD1 A:TRP279 4.3 12.8 1.0
CE2 A:TRP486 4.4 8.3 1.0
CZ2 A:TRP485 4.4 9.9 1.0
HD1 A:TRP485 4.4 12.1 1.0
CZ2 A:TRP182 4.5 7.2 1.0
O A:ASP507 4.5 10.9 1.0
HE1 A:TRP486 4.5 10.8 1.0
CG A:ASP507 4.6 10.1 1.0
HE1 A:TRP182 4.6 10.5 1.0
HG2 A:ARG186 4.7 11.3 1.0
C A:ASP507 4.7 9.2 1.0
NE1 A:TRP486 4.8 9.0 1.0
O A:HOH1141 4.8 10.4 1.0
HD3 A:ARG489 4.8 11.6 1.0
HA A:TRP279 4.8 7.6 1.0
CA A:ASP507 4.8 7.9 1.0
HG3 A:ARG489 4.9 11.6 1.0
OD2 A:ASP507 5.0 10.6 1.0
CD A:ARG489 5.0 9.7 1.0
NH1 A:ARG489 5.0 9.6 1.0

Chlorine binding site 2 out of 2 in 7q27

Go back to Chlorine Binding Sites List in 7q27
Chlorine binding site 2 out of 2 in the Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD011


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 in Complex with Dual Ace/Nep Inhibitor AD011 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl709

b:11.5
occ:1.00
HH A:TYR224 2.2 13.8 1.0
HE A:ARG522 2.3 11.0 1.0
HB3 A:ARG522 2.7 9.5 1.0
HH21 A:ARG522 2.8 14.1 1.0
HB2 A:PRO519 2.8 8.6 1.0
H A:ARG522 2.8 7.6 1.0
HG22 A:ILE521 3.0 11.2 1.0
HE1 A:TYR224 3.0 9.3 1.0
HB2 A:PRO407 3.1 12.9 1.0
OH A:TYR224 3.1 11.5 1.0
O A:HOH1212 3.1 13.4 1.0
NE A:ARG522 3.2 9.2 1.0
HG2 A:PRO407 3.4 12.1 1.0
HE3 A:MET223 3.5 17.2 1.0
N A:ARG522 3.5 6.4 1.0
CB A:ARG522 3.5 7.9 1.0
NH2 A:ARG522 3.6 11.7 1.0
HB3 A:PRO519 3.6 8.6 1.0
CB A:PRO519 3.6 7.2 1.0
HG23 A:ILE521 3.6 11.2 1.0
CE1 A:TYR224 3.7 7.8 1.0
CB A:PRO407 3.7 10.8 1.0
HG2 A:ARG522 3.7 9.3 1.0
HE1 A:MET223 3.7 17.2 1.0
CG2 A:ILE521 3.7 9.4 1.0
HB3 A:PRO407 3.8 12.9 1.0
CZ A:TYR224 3.8 8.3 1.0
CZ A:ARG522 3.8 11.5 1.0
CA A:ARG522 3.9 7.7 1.0
CG A:ARG522 4.0 7.8 1.0
HA A:ARG522 4.0 9.2 1.0
CG A:PRO407 4.0 10.0 1.0
CE A:MET223 4.0 14.3 1.0
H A:ILE521 4.1 7.7 1.0
CD A:ARG522 4.2 10.3 1.0
HG2 A:PRO519 4.2 9.9 1.0
HG21 A:ILE521 4.2 11.2 1.0
HB2 A:ARG522 4.3 9.5 1.0
HH22 A:ARG522 4.3 14.1 1.0
N A:ILE521 4.4 6.4 1.0
C A:ILE521 4.5 5.7 1.0
CG A:PRO519 4.5 8.3 1.0
HE2 A:MET223 4.5 17.2 1.0
C A:PRO519 4.6 7.4 1.0
HG3 A:PRO407 4.6 12.1 1.0
CA A:PRO519 4.7 6.4 1.0
HD2 A:PRO407 4.7 11.5 1.0
HD2 A:ARG522 4.8 12.4 1.0
O A:HOH1001 4.8 12.0 1.0
HD3 A:ARG522 4.8 12.4 1.0
O A:PRO519 4.8 8.5 1.0
CA A:ILE521 4.8 7.1 1.0
N A:TYR520 4.8 8.4 1.0
CB A:ILE521 4.9 7.7 1.0
CD1 A:TYR224 4.9 10.7 1.0
HG3 A:ARG522 4.9 9.3 1.0
H A:TYR520 4.9 10.0 1.0
HB2 A:MET223 5.0 14.1 1.0
CD A:PRO407 5.0 9.6 1.0

Reference:

L.B.Arendse, G.E.Cozier, C.J.Eyermann, G.S.Basarab, S.L.Schwager, K.Chibale, K.R.Acharya, E.D.Sturrock. Probing the Requirements For Dual Angiotensin-Converting Enzyme C-Domain Selective/Neprilysin Inhibition. J.Med.Chem. V. 65 3371 2022.
ISSN: ISSN 0022-2623
PubMed: 35113565
DOI: 10.1021/ACS.JMEDCHEM.1C01924
Page generated: Sun Jul 13 06:08:38 2025

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