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Chlorine in PDB 1r42: Native Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2)

Protein crystallography data

The structure of Native Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2), PDB code: 1r42 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) 46.74 / 2.20
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 103.638, 89.478, 112.399, 90.00, 109.15, 90.00
R / Rfree (%) n/a / n/a

Other elements in 1r42:

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

Zinc (Zn) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Native Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2) (pdb code 1r42). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Native Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2), PDB code: 1r42:

Chlorine binding site 1 out of 1 in 1r42

Go back to Chlorine Binding Sites List in 1r42
Chlorine binding site 1 out of 1 in the Native 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 Native Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl803

b:44.4
occ:1.00
NH1 A:ARG169 3.2 34.9 1.0
NE A:ARG169 3.2 41.4 1.0
O A:HOH897 3.3 47.1 1.0
NE1 A:TRP477 3.5 45.4 1.0
CZ A:ARG169 3.7 40.7 1.0
O A:HOH835 3.7 47.0 1.0
CZ2 A:TRP478 3.7 38.1 1.0
CB A:ASP499 3.7 45.2 1.0
CZ2 A:TRP477 3.9 41.2 1.0
O A:ASP499 3.9 45.3 1.0
CH2 A:TRP478 4.0 37.0 1.0
CE2 A:TRP477 4.0 44.3 1.0
C A:ASP499 4.3 43.9 1.0
CD A:ARG169 4.4 38.7 1.0
CE A:LYS481 4.5 55.0 1.0
CZ2 A:TRP165 4.5 42.2 1.0
CA A:ASP499 4.5 44.8 1.0
CG A:ASP499 4.5 46.6 1.0
CD1 A:TRP477 4.7 46.4 1.0
CE2 A:TRP478 4.7 38.5 1.0
OD1 A:ASP499 4.8 44.6 1.0
CD1 A:TRP271 4.9 39.7 1.0
OG A:SER502 5.0 45.3 1.0
NH2 A:ARG169 5.0 36.8 1.0

Reference:

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
Page generated: Sat Dec 12 08:47:48 2020

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