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Chlorine in PDB 7z70: Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Fosinoprilat

Enzymatic activity of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Fosinoprilat

All present enzymatic activity of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Fosinoprilat:
3.4.15.1;

Protein crystallography data

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Fosinoprilat, PDB code: 7z70 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) 52.15 / 1.85
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.563, 85.987, 134.686, 90, 90, 90
R / Rfree (%) 17.4 / 21.3

Other elements in 7z70:

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Fosinoprilat 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 Fosinoprilat (pdb code 7z70). 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 Fosinoprilat, PDB code: 7z70:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 7z70

Go back to Chlorine Binding Sites List in 7z70
Chlorine binding site 1 out of 2 in the Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Fosinoprilat


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 Fosinoprilat within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl711

b:17.9
occ:1.00
HE A:ARG186 2.4 20.4 1.0
HE1 A:TRP485 2.4 21.6 1.0
HH21 A:ARG186 2.5 20.8 1.0
HH21 A:ARG489 2.7 21.6 1.0
HB3 A:ASP507 2.9 19.4 1.0
HZ2 A:TRP486 3.1 19.1 1.0
NE A:ARG186 3.2 17.0 1.0
NH2 A:ARG489 3.2 18.0 1.0
NH2 A:ARG186 3.3 17.3 1.0
NE1 A:TRP485 3.3 18.0 1.0
HE A:ARG489 3.4 19.7 1.0
O A:HOH967 3.4 20.4 1.0
CZ2 A:TRP486 3.6 15.9 1.0
HH22 A:ARG489 3.6 21.6 1.0
CZ A:ARG186 3.7 15.3 1.0
NE A:ARG489 3.8 16.4 1.0
CB A:ASP507 3.8 16.1 1.0
HZ2 A:TRP485 3.8 20.5 1.0
CZ A:ARG489 3.8 14.0 1.0
HZ2 A:TRP182 3.8 16.6 1.0
HB2 A:ASP507 3.9 19.4 1.0
HH22 A:ARG186 4.0 20.8 1.0
HH2 A:TRP486 4.0 19.6 1.0
CH2 A:TRP486 4.1 16.3 1.0
CE2 A:TRP485 4.2 16.7 1.0
HD3 A:ARG186 4.3 20.5 1.0
CD1 A:TRP485 4.3 15.3 1.0
CE2 A:TRP486 4.3 14.2 1.0
CZ2 A:TRP485 4.3 17.1 1.0
CD A:ARG186 4.3 17.1 1.0
HD1 A:TRP485 4.4 18.4 1.0
HD1 A:TRP279 4.4 17.1 1.0
O A:ASP507 4.5 17.5 1.0
CZ2 A:TRP182 4.5 13.9 1.0
HE1 A:TRP486 4.5 17.1 1.0
CG A:ASP507 4.6 16.7 1.0
HE1 A:TRP182 4.6 21.0 1.0
C A:ASP507 4.7 16.0 1.0
HG3 A:ARG489 4.7 17.6 1.0
NE1 A:TRP486 4.7 14.2 1.0
HG2 A:ARG186 4.7 20.3 1.0
HD3 A:ARG489 4.8 18.1 1.0
CA A:ASP507 4.8 16.2 1.0
CD A:ARG489 4.8 15.1 1.0
HA A:TRP279 4.9 17.8 1.0
NH1 A:ARG489 4.9 15.8 1.0
O A:HOH981 4.9 17.1 1.0
OD2 A:ASP507 4.9 17.7 1.0
HA A:ASP507 5.0 19.4 1.0

Chlorine binding site 2 out of 2 in 7z70

Go back to Chlorine Binding Sites List in 7z70
Chlorine binding site 2 out of 2 in the Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Fosinoprilat


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 Fosinoprilat within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl712

b:19.1
occ:1.00
HE A:ARG522 2.4 16.3 1.0
HB3 A:ARG522 2.7 14.8 1.0
HB2 A:PRO519 2.9 15.8 1.0
HH21 A:ARG522 2.9 21.2 1.0
H A:ARG522 2.9 16.1 1.0
HE1 A:TYR224 3.0 19.9 1.0
O A:HOH1037 3.0 17.6 1.0
OH A:TYR224 3.0 15.4 1.0
HB2 A:PRO407 3.0 20.3 1.0
HG22 A:ILE521 3.0 22.7 1.0
HG2 A:PRO407 3.2 19.9 1.0
NE A:ARG522 3.2 13.6 1.0
HG23 A:ILE521 3.4 22.7 1.0
CB A:ARG522 3.5 12.3 1.0
N A:ARG522 3.6 13.4 1.0
CE1 A:TYR224 3.6 16.6 1.0
HH A:TYR224 3.6 18.5 1.0
HB3 A:PRO519 3.6 15.8 1.0
CB A:PRO407 3.7 16.9 1.0
NH2 A:ARG522 3.7 17.6 1.0
CB A:PRO519 3.7 13.2 1.0
CG2 A:ILE521 3.7 18.9 1.0
HG2 A:ARG522 3.7 16.3 1.0
CZ A:TYR224 3.7 16.1 1.0
HB3 A:PRO407 3.8 20.3 1.0
CG A:PRO407 3.8 16.6 1.0
CZ A:ARG522 3.9 17.6 1.0
CA A:ARG522 4.0 13.0 1.0
CG A:ARG522 4.0 13.6 1.0
HA A:ARG522 4.0 15.6 1.0
HG2 A:PRO519 4.1 17.0 1.0
HG21 A:ILE521 4.1 22.7 1.0
H A:ILE521 4.2 14.4 1.0
CD A:ARG522 4.2 13.4 1.0
HB2 A:ARG522 4.3 14.8 1.0
SD A:MET223 4.4 26.6 1.0
HH22 A:ARG522 4.4 21.2 1.0
CG A:PRO519 4.5 14.2 1.0
HD2 A:PRO407 4.5 21.4 1.0
HG3 A:PRO407 4.5 19.9 1.0
N A:ILE521 4.5 12.0 1.0
HE1 A:MET223 4.5 32.7 1.0
C A:ILE521 4.6 12.6 1.0
HB2 A:MET223 4.7 22.5 1.0
C A:PRO519 4.7 16.4 1.0
HE2 A:MET223 4.8 32.7 1.0
HD3 A:ARG522 4.8 16.1 1.0
CD A:PRO407 4.8 17.8 1.0
HD2 A:ARG522 4.8 16.1 1.0
CD1 A:TYR224 4.8 16.4 1.0
CE A:MET223 4.8 27.3 1.0
CA A:PRO519 4.8 13.1 1.0
O A:HOH1003 4.8 14.7 1.0
CB A:ILE521 4.9 14.1 1.0
CA A:ILE521 4.9 14.1 1.0
O A:PRO519 4.9 11.6 1.0
HG3 A:ARG522 4.9 16.3 1.0
N A:TYR520 5.0 14.3 1.0

Reference:

G.E.Cozier, E.C.Newby, S.L.U.Schwager, R.E.Isaac, E.D.Sturrock, K.R.Acharya. Structural Basis For the Inhibition of Human Angiotensin-1 Converting Enzyme By Fosinoprilat. Febs J. V. 289 6659 2022.
ISSN: ISSN 1742-464X
PubMed: 35653492
DOI: 10.1111/FEBS.16543
Page generated: Sun Jul 13 08:42:52 2025

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