Magnesium in PDB 6qs1: Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Bppb

All present enzymatic activity of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Bppb:
3.4.15.1;

The structure of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Bppb, PDB code: 6qs1 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)	74.05 / 1.80
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	72.682, 77.070, 82.363, 88.86, 64.59, 75.03
R / Rfree (%)	20.2 / 23.2

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

Zinc	(Zn)	2 atoms
Chlorine	(Cl)	4 atoms

The binding sites of Magnesium atom in the Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Bppb (pdb code 6qs1). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Bppb, PDB code: 6qs1:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Bppb


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Bppb within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg725 b:39.0 occ:0.68 OE2 A:GLU262 2.0 38.1 0.5 OD1 A:ASN263 2.1 37.7 1.0 OE1 A:GLU262 2.3 36.1 0.5 O A:HOH991 2.4 39.3 1.0 CD A:GLU262 2.4 36.2 0.5 OD1 A:ASP354 2.6 44.8 1.0 O A:HOH988 2.7 46.2 1.0 CG A:ASN263 3.0 37.9 1.0 HD21 A:ASN263 3.3 46.2 1.0 CG A:ASP354 3.5 40.1 1.0 ND2 A:ASN263 3.6 38.5 1.0 HB3 A:ASP354 3.6 42.7 1.0 HA A:ASN263 3.8 39.5 1.0 CG A:GLU262 4.0 33.9 0.5 H A:ASP354 4.0 39.1 1.0 HG2 A:GLU262 4.1 40.5 0.5 CB A:ASP354 4.1 35.5 1.0 HB A:THR352 4.2 42.4 1.0 HG1 A:THR352 4.3 41.3 1.0 CB A:ASN263 4.3 36.6 1.0 HG3 A:GLU262 4.3 40.6 0.5 HG3 A:GLU262 4.3 40.5 0.5 HB1 A:ALA148 4.3 49.7 1.0 HG2 A:GLU262 4.3 40.6 0.5 HD22 A:ASN263 4.4 46.2 1.0 CA A:ASN263 4.4 32.9 1.0 OD2 A:ASP354 4.4 47.4 1.0 N A:ASN263 4.6 32.3 1.0 O A:HOH888 4.7 37.1 1.0 CG A:GLU262 4.7 33.7 0.5 HB2 A:GLU262 4.7 39.3 0.5 H A:ASN263 4.7 38.8 1.0 HB3 A:ASN263 4.7 44.0 1.0 HB2 A:ASP354 4.8 42.7 1.0 N A:ASP354 4.8 32.6 1.0 HG1 A:THR280 4.8 46.1 1.0 OG1 A:THR352 4.8 34.4 1.0 HG21 A:THR352 4.9 41.1 1.0 HB2 A:ASN263 4.9 44.0 1.0 CB A:THR352 4.9 35.3 1.0 CB A:GLU262 5.0 32.7 0.5 C A:GLU262 5.0 31.8 0.5

Magnesium binding site 2 out of 2 in the Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Bppb


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Bppb within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg717 b:47.9 occ:1.00 OE2 B:GLU262 1.9 47.9 1.0 O B:HOH900 2.0 38.8 1.0 O B:HOH954 2.4 43.1 1.0 O B:HOH1029 2.7 48.5 1.0 CD B:GLU262 3.1 44.3 1.0 OD1 B:ASN263 3.1 39.6 1.0 OD2 B:ASP354 3.1 56.0 1.0 HG B:SER260 3.5 50.5 1.0 CG B:ASP354 3.7 49.7 1.0 HB2 B:ASP354 3.7 45.2 1.0 HG2 B:GLU262 3.8 44.9 1.0 OG B:SER260 3.9 42.1 1.0 OE1 B:GLU262 3.9 39.6 1.0 HB3 B:ASP354 4.0 45.2 1.0 CG B:GLU262 4.0 37.4 1.0 HD21 B:ASN263 4.0 47.4 1.0 CG B:ASN263 4.0 39.5 1.0 CB B:ASP354 4.1 37.6 1.0 HG3 B:GLU262 4.2 44.9 1.0 O B:HOH1019 4.2 43.5 1.0 O B:HOH995 4.3 44.5 1.0 O B:HOH1003 4.3 44.4 1.0 O B:HOH901 4.3 32.3 1.0 OD1 B:ASP354 4.4 50.1 1.0 ND2 B:ASN263 4.4 39.5 1.0 OD2 B:ASP255 4.5 35.3 1.0 HB2 B:ASP255 4.5 35.7 1.0 O B:HOH1031 4.7 40.8 1.0 H B:ASN263 4.7 37.0 1.0 O B:HOH838 5.0 32.7 1.0

E.D.Sturrock, L.Lubbe, G.E.Cozier, S.L.U.Schwager, A.T.Arowolo, L.B.Arendse, E.Belcher, K.R.Acharya. Structural Basis For the C-Domain-Selective Angiotensin-Converting Enzyme Inhibition By Bradykinin-Potentiating Peptide B (Bppb). Biochem.J. V. 476 1553 2019.
ISSN: ESSN 1470-8728
PubMed: 31072910
DOI: 10.1042/BCJ20190290