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Chlorine in PDB 7q3y: Structure of Full-Length, Monomeric, Soluble Somatic Angiotensin I- Converting Enzyme Showing the N- and C-Terminal Ellipsoid Domains

Enzymatic activity of Structure of Full-Length, Monomeric, Soluble Somatic Angiotensin I- Converting Enzyme Showing the N- and C-Terminal Ellipsoid Domains

All present enzymatic activity of Structure of Full-Length, Monomeric, Soluble Somatic Angiotensin I- Converting Enzyme Showing the N- and C-Terminal Ellipsoid Domains:
3.4.15.1;

Other elements in 7q3y:

The structure of Structure of Full-Length, Monomeric, Soluble Somatic Angiotensin I- Converting Enzyme Showing the N- and C-Terminal Ellipsoid Domains also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of Full-Length, Monomeric, Soluble Somatic Angiotensin I- Converting Enzyme Showing the N- and C-Terminal Ellipsoid Domains (pdb code 7q3y). 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 Structure of Full-Length, Monomeric, Soluble Somatic Angiotensin I- Converting Enzyme Showing the N- and C-Terminal Ellipsoid Domains, PDB code: 7q3y:

Chlorine binding site 1 out of 1 in 7q3y

Go back to Chlorine Binding Sites List in 7q3y
Chlorine binding site 1 out of 1 in the Structure of Full-Length, Monomeric, Soluble Somatic Angiotensin I- Converting Enzyme Showing the N- and C-Terminal Ellipsoid Domains


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Full-Length, Monomeric, Soluble Somatic Angiotensin I- Converting Enzyme Showing the N- and C-Terminal Ellipsoid Domains within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1302

b:89.0
occ:1.00
HH21 A:ARG1098 2.6 107.5 1.0
HG3 A:PRO1095 2.8 102.0 1.0
HG2 A:PRO983 3.2 111.2 1.0
HG2 A:PRO1095 3.4 102.0 1.0
NH2 A:ARG1098 3.4 107.5 1.0
CG A:PRO1095 3.5 102.0 1.0
HE A:ARG1098 3.5 107.5 1.0
HB2 A:PRO1095 3.6 102.0 1.0
HH A:TYR800 3.6 116.0 1.0
HB3 A:PRO983 3.7 111.2 1.0
CG A:PRO983 3.9 111.2 1.0
CB A:PRO1095 3.9 102.0 1.0
HG3 A:PRO983 3.9 111.2 1.0
HH22 A:ARG1098 3.9 107.5 1.0
HB2 A:PRO983 4.0 111.2 1.0
CB A:PRO983 4.0 111.2 1.0
HB3 A:PRO1095 4.1 102.0 1.0
HB3 A:ARG1098 4.1 107.5 1.0
HB2 A:MET799 4.1 114.6 1.0
NE A:ARG1098 4.2 107.5 1.0
HG3 A:MET799 4.2 114.6 1.0
HE1 A:TYR800 4.2 116.0 1.0
CZ A:ARG1098 4.3 107.5 1.0
OH A:TYR800 4.3 116.0 1.0
HB3 A:TRP796 4.4 117.1 1.0
HB3 A:MET799 4.6 114.6 1.0
CE1 A:TYR800 4.7 116.0 1.0
CB A:MET799 4.7 114.6 1.0
HG22 A:ILE1097 4.7 108.1 1.0
CZ A:TYR800 4.8 116.0 1.0
CD A:PRO1095 4.8 102.0 1.0
CG A:MET799 4.9 114.6 1.0
HA A:TRP796 5.0 117.1 1.0
H A:ARG1098 5.0 107.5 1.0
O A:TRP796 5.0 117.1 1.0

Reference:

L.Lubbe, B.T.Sewell, J.D.Woodward, E.D.Sturrock. Cryo-Em Reveals Mechanisms of Angiotensin I-Converting Enzyme Allostery and Dimerization. Embo J. V. 41 10550 2022.
ISSN: ESSN 1460-2075
PubMed: 35818993
DOI: 10.15252/EMBJ.2021110550
Page generated: Sun Jul 13 06:09:52 2025

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