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Zinc 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:

Chlorine (Cl) 1 atom

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total only one binding site of Zinc 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:

Zinc binding site 1 out of 1 in 7q3y

Go back to Zinc Binding Sites List in 7q3y
Zinc 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 Zinc with other atoms in the Zn 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:Zn1301

b:148.5
occ:1.00
OE1 A:GLU389 2.0 102.1 1.0
O A:HOH2001 2.1 105.6 1.0
H2 A:HOH2001 2.2 105.6 1.0
NE2 A:HIS361 2.3 113.5 1.0
NE2 A:HIS365 2.3 113.5 1.0
H1 A:HOH2001 2.3 105.6 1.0
CD A:GLU389 3.0 102.1 1.0
CD2 A:HIS365 3.1 113.5 1.0
CD2 A:HIS361 3.1 113.5 1.0
HD2 A:HIS365 3.2 113.5 1.0
HD2 A:HIS361 3.2 113.5 1.0
CE1 A:HIS361 3.3 113.5 1.0
CE1 A:HIS365 3.4 113.5 1.0
OE2 A:GLU389 3.5 102.1 1.0
HE1 A:HIS361 3.6 113.5 1.0
HE1 A:HIS365 3.6 113.5 1.0
OE2 A:GLU362 3.8 123.3 1.0
HA A:GLU389 4.1 102.1 1.0
HG2 A:GLU389 4.2 102.1 1.0
CG A:GLU389 4.3 102.1 1.0
CG A:HIS365 4.3 113.5 1.0
CG A:HIS361 4.3 113.5 1.0
ND1 A:HIS361 4.4 113.5 1.0
ND1 A:HIS365 4.4 113.5 1.0
CD A:GLU362 4.8 123.3 1.0
HG3 A:GLU389 4.9 102.1 1.0
HA3 A:GLY392 4.9 116.0 1.0
CA A:GLU389 5.0 102.1 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: Wed Oct 30 09:33:53 2024

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