Calcium in PDB 7z6z: Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Fosinoprilat

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Fosinoprilat, PDB code: 7z6z 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)	63.46 / 1.75
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	72.575, 77.8, 81.592, 88.92, 64.62, 74.81
R / Rfree (%)	17.2 / 20

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Fosinoprilat also contains other interesting chemical elements:

Chlorine	(Cl)	2 atoms
Zinc	(Zn)	2 atoms
Sodium	(Na)	1 atom

The binding sites of Calcium atom in the Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Fosinoprilat (pdb code 7z6z). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Fosinoprilat, PDB code: 7z6z:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Fosinoprilat


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Fosinoprilat within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca722 b:65.5 occ:1.00 OD1 A:ASN263 2.4 37.4 1.0 O A:HOH1034 2.4 39.4 1.0 O A:HOH1095 2.4 45.8 1.0 OD1 A:ASP354 2.6 39.7 1.0 OE1 A:GLU262 2.8 55.8 1.0 OE2 A:GLU262 3.0 47.1 1.0 CD A:GLU262 3.3 50.4 1.0 O A:HOH1137 3.4 52.2 1.0 CG A:ASP354 3.5 36.9 1.0 CG A:ASN263 3.5 34.1 1.0 HB3 A:ASP354 3.8 43.5 1.0 HB A:THR352 3.8 35.9 1.0 H A:ASP354 3.8 32.5 1.0 HA A:ASN263 3.9 35.2 1.0 HG1 A:THR280 3.9 34.8 1.0 HD21 A:ASN263 4.0 40.9 1.0 O A:HOH979 4.1 42.2 1.0 ND2 A:ASN263 4.2 34.1 1.0 CB A:ASP354 4.2 36.3 1.0 HG1 A:THR352 4.3 33.3 1.0 OD2 A:ASP354 4.4 43.2 1.0 CA A:ASN263 4.6 29.4 1.0 HB1 A:ALA148 4.6 43.7 1.0 CB A:ASN263 4.6 31.7 1.0 CB A:THR352 4.6 29.9 1.0 N A:ASP354 4.6 27.1 1.0 OG1 A:THR280 4.7 29.0 1.0 HG21 A:THR352 4.7 33.4 1.0 O A:HOH898 4.7 39.2 1.0 CG A:GLU262 4.8 38.1 1.0 OG1 A:THR352 4.8 27.8 1.0 H A:MET353 4.9 33.1 1.0 HB3 A:MET353 4.9 33.6 1.0 N A:ASN263 4.9 26.8 1.0 HB2 A:ASP354 4.9 43.5 1.0 HB3 A:ASN263 5.0 38.0 1.0 NA A:NA723 5.0 46.3 1.0

Calcium binding site 2 out of 3 in the Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Fosinoprilat


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Fosinoprilat within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca722 b:50.7 occ:1.00 O B:ACT712 2.6 61.2 1.0 O2 B:EDO715 2.6 39.3 1.0 O2 B:EDO716 2.7 40.8 1.0 O1 B:EDO716 2.9 45.8 1.0 O B:HOH1049 2.9 52.7 1.0 O1 B:EDO715 2.9 51.2 1.0 H12 B:EDO716 3.3 50.5 1.0 HO2 B:EDO716 3.3 48.9 1.0 C1 B:EDO716 3.3 42.1 1.0 C2 B:EDO716 3.3 43.0 1.0 HO2 B:EDO715 3.4 47.1 1.0 H21 B:EDO716 3.4 51.5 1.0 C2 B:EDO715 3.5 41.9 1.0 H21 B:EDO715 3.5 50.2 1.0 HO1 B:EDO716 3.5 54.9 1.0 HO1 B:EDO715 3.6 61.4 1.0 C B:ACT712 3.6 53.1 1.0 C1 B:EDO715 3.7 44.0 1.0 H2 B:ACT712 4.0 63.0 1.0 H12 B:EDO715 4.2 52.7 1.0 CH3 B:ACT712 4.3 52.5 1.0 H22 B:EDO716 4.4 51.5 1.0 H11 B:EDO716 4.4 50.5 1.0 H22 B:EDO715 4.5 50.2 1.0 OXT B:ACT712 4.5 48.7 1.0 H3 B:ACT712 4.6 63.0 1.0 H11 B:EDO715 4.6 52.7 1.0

Calcium binding site 3 out of 3 in the Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Fosinoprilat


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Crystal Structure of Angiotensin-1 Converting Enzyme N-Domain in Complex with Fosinoprilat within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca723 b:55.5 occ:1.00 O B:HOH812 2.1 34.5 1.0 O B:HOH911 2.2 40.2 1.0 OE2 B:GLU262 2.4 45.1 1.0 O B:HOH1068 2.5 36.8 1.0 OD1 B:ASN263 2.8 34.1 1.0 OD2 B:ASP354 3.0 48.5 1.0 CD B:GLU262 3.3 40.0 1.0 HB2 B:ASP354 3.5 40.7 1.0 CG B:ASP354 3.5 36.5 1.0 HG2 B:GLU262 3.7 37.3 1.0 OG B:SER260 3.8 40.5 1.0 HG B:SER260 3.8 48.6 1.0 CG B:ASN263 3.8 32.7 1.0 HD22 B:ASN263 3.9 37.6 1.0 CB B:ASP354 3.9 33.9 1.0 HB3 B:ASP354 4.0 40.7 1.0 CG B:GLU262 4.0 31.1 1.0 HG3 B:GLU262 4.1 37.3 1.0 OE1 B:GLU262 4.2 34.7 1.0 ND2 B:ASN263 4.2 31.4 1.0 O B:HOH1086 4.3 39.0 1.0 O B:HOH908 4.3 26.2 1.0 OD1 B:ASP354 4.3 37.0 1.0 O B:HOH804 4.4 37.9 1.0 OD2 B:ASP255 4.4 24.1 1.0 HB2 B:ASP255 4.4 30.4 1.0 O B:HOH1083 4.5 38.6 1.0 O B:HOH891 4.6 45.7 1.0 H B:ASN263 4.8 30.5 1.0 O B:HOH973 4.8 24.7 1.0

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