Chlorine in PDB 1r4l: Inhibitor Bound Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2)

The structure of Inhibitor Bound Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2), PDB code: 1r4l was solved by P.Towler, B.Staker, S.G.Prasad, S.Menon, D.Ryan, J.Tang, T.Parsons, M.Fisher, D.Williams, N.A.Dales, M.A.Patane, M.W.Pantoliano, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.26 / 3.00
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	100.531, 86.509, 105.858, 90.00, 103.65, 90.00
R / Rfree (%)	n/a / n/a

The structure of Inhibitor Bound Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2) also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Chlorine atom in the Inhibitor Bound Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2) (pdb code 1r4l). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Inhibitor Bound Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2), PDB code: 1r4l:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Inhibitor Bound Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Inhibitor Bound Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl802 b:54.4 occ:1.00 NE A:ARG169 2.9 51.9 1.0 CB A:ASP499 3.3 69.1 1.0 NH1 A:ARG169 3.3 47.0 1.0 CZ A:ARG169 3.6 54.0 1.0 CZ2 A:TRP478 3.9 32.9 1.0 NE1 A:TRP477 3.9 70.5 1.0 CD A:ARG169 3.9 50.0 1.0 CG A:ASP499 4.0 70.7 1.0 CH2 A:TRP478 4.0 35.0 1.0 O A:ASP499 4.0 72.9 1.0 C A:ASP499 4.2 68.7 1.0 CA A:ASP499 4.2 69.2 1.0 OD1 A:ASP499 4.2 67.1 1.0 CZ2 A:TRP165 4.4 53.7 1.0 CE2 A:TRP477 4.6 72.6 1.0 CZ2 A:TRP477 4.6 71.1 1.0 OD2 A:ASP499 4.8 72.7 1.0 CD1 A:TRP271 4.9 44.7 1.0 NH2 A:ARG169 4.9 53.9 1.0 CE2 A:TRP478 4.9 33.2 1.0 CD1 A:TRP477 4.9 66.7 1.0 N A:PRO500 5.0 66.2 1.0

Chlorine binding site 2 out of 3 in the Inhibitor Bound Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Inhibitor Bound Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl804 b:51.7 occ:1.00 CL24 A:XX5804 0.0 51.7 1.0 C23 A:XX5804 1.8 49.0 1.0 OD2 A:ASP368 2.7 72.6 1.0 C25 A:XX5804 2.7 41.9 1.0 C22 A:XX5804 2.8 41.9 1.0 OD1 A:ASP368 3.2 79.8 1.0 CG A:ASP368 3.2 74.4 1.0 CE A:MET360 3.7 61.5 1.0 CG A:PRO346 3.9 49.4 1.0 C27 A:XX5804 4.1 45.7 1.0 C21 A:XX5804 4.1 40.4 1.0 CD A:LYS363 4.3 74.5 1.0 O A:CYS361 4.4 67.2 1.0 CB A:ASP368 4.5 72.2 1.0 C26 A:XX5804 4.6 40.7 1.0 CG A:MET360 4.6 62.6 1.0 CD A:PRO346 4.7 50.3 1.0 SD A:MET360 4.9 65.8 1.0 CA A:ASP368 4.9 70.4 1.0

Chlorine binding site 3 out of 3 in the Inhibitor Bound Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Inhibitor Bound Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl804 b:35.7 occ:1.00 CL28 A:XX5804 0.0 35.7 1.0 C27 A:XX5804 1.8 45.7 1.0 C25 A:XX5804 2.8 41.9 1.0 C26 A:XX5804 2.9 40.7 1.0 OD1 A:ASN149 3.9 62.4 1.0 CA A:HIS345 4.0 56.3 1.0 N A:HIS345 4.0 59.0 1.0 OE1 A:GLU145 4.1 71.9 1.0 C23 A:XX5804 4.1 49.0 1.0 C A:CYS344 4.1 61.0 1.0 O A:CYS344 4.2 58.6 1.0 C21 A:XX5804 4.2 40.4 1.0 CB A:GLU145 4.2 57.5 1.0 CG A:GLU145 4.3 61.8 1.0 CD A:GLU145 4.4 68.5 1.0 ND1 A:HIS345 4.5 61.2 1.0 CB A:CYS344 4.5 66.7 1.0 CD A:PRO346 4.6 50.3 1.0 C22 A:XX5804 4.7 41.9 1.0 CB A:HIS345 4.7 55.2 1.0 CA A:CYS344 4.9 64.0 1.0 CG A:HIS345 4.9 58.9 1.0

P.Towler, B.Staker, S.G.Prasad, S.Menon, J.Tang, T.Parsons, D.Ryan, M.Fisher, D.Williams, N.A.Dales, M.A.Patane, M.W.Pantoliano. ACE2 X-Ray Structures Reveal A Large Hinge-Bending Motion Important For Inhibitor Binding and Catalysis. J.Biol.Chem. V. 279 17996 2004.
ISSN: ISSN 0021-9258
PubMed: 14754895
DOI: 10.1074/JBC.M311191200