Zinc 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:

Chlorine

(Cl)

3 atoms

The binding sites of Zinc 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 Zinc atom.
In total only one binding site of Zinc was determined in the Inhibitor Bound Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2), PDB code: 1r4l:

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


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn 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:Zn803 b:37.7 occ:1.00 O1 A:XX5804 2.0 34.2 1.0 NE2 A:HIS374 2.0 28.3 1.0 OE1 A:GLU402 2.1 23.7 1.0 NE2 A:HIS378 2.3 58.0 1.0 C2 A:XX5804 2.6 38.0 1.0 O3 A:XX5804 2.6 35.4 1.0 CD A:GLU402 3.0 31.3 1.0 CE1 A:HIS374 3.0 28.0 1.0 CD2 A:HIS374 3.0 26.6 1.0 CD2 A:HIS378 3.1 57.7 1.0 OE2 A:GLU402 3.2 28.4 1.0 CE1 A:HIS378 3.3 55.6 1.0 C4 A:XX5804 4.0 43.4 1.0 OE2 A:GLU375 4.1 53.5 1.0 ND1 A:HIS374 4.1 30.4 1.0 CG A:HIS374 4.2 31.5 1.0 CG A:HIS378 4.2 53.9 1.0 ND1 A:HIS378 4.3 55.3 1.0 CG A:GLU402 4.4 29.8 1.0 CA A:GLU402 4.5 40.3 1.0 N9 A:XX5804 4.7 49.8 1.0 CB A:GLU402 4.7 35.2 1.0 CE1 A:TYR515 4.7 27.7 1.0 C10 A:XX5804 4.8 52.3 1.0 OH A:TYR515 4.9 30.8 1.0 O12 A:XX5804 5.0 50.9 1.0 CD A:GLU375 5.0 54.8 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