Zinc in PDB 7q49: Local Refinement Structure of the N-Domain of Full-Length, Monomeric, Soluble Somatic Angiotensin I-Converting Enzyme

Enzymatic activity of Local Refinement Structure of the N-Domain of Full-Length, Monomeric, Soluble Somatic Angiotensin I-Converting Enzyme

All present enzymatic activity of Local Refinement Structure of the N-Domain of Full-Length, Monomeric, Soluble Somatic Angiotensin I-Converting Enzyme:
3.4.15.1;

Zinc Binding Sites:

The binding sites of Zinc atom in the Local Refinement Structure of the N-Domain of Full-Length, Monomeric, Soluble Somatic Angiotensin I-Converting Enzyme (pdb code 7q49). 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 Local Refinement Structure of the N-Domain of Full-Length, Monomeric, Soluble Somatic Angiotensin I-Converting Enzyme, PDB code: 7q49:

Zinc binding site 1 out of 1 in 7q49

Go back to Zinc Binding Sites List in 7q49
Zinc binding site 1 out of 1 in the Local Refinement Structure of the N-Domain of Full-Length, Monomeric, Soluble Somatic Angiotensin I-Converting Enzyme


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Local Refinement Structure of the N-Domain of Full-Length, Monomeric, Soluble Somatic Angiotensin I-Converting Enzyme within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1301

b:186.6
occ:1.00
OE1 A:GLU389 2.0 141.3 1.0
O A:HOH2001 2.1 153.8 1.0
NE2 A:HIS365 2.3 142.5 1.0
NE2 A:HIS361 2.3 149.9 1.0
H2 A:HOH2001 2.4 153.8 1.0
H1 A:HOH2001 2.6 153.8 1.0
CD A:GLU389 3.1 141.3 1.0
CD2 A:HIS365 3.1 142.5 1.0
HD2 A:HIS365 3.2 142.5 1.0
CD2 A:HIS361 3.2 149.9 1.0
CE1 A:HIS361 3.3 149.9 1.0
CE1 A:HIS365 3.3 142.5 1.0
HD2 A:HIS361 3.3 149.9 1.0
HE1 A:HIS361 3.5 149.9 1.0
HE1 A:HIS365 3.6 142.5 1.0
OE2 A:GLU389 3.7 141.3 1.0
OE2 A:GLU362 4.1 151.4 1.0
HA A:GLU389 4.1 141.3 1.0
HG2 A:GLU389 4.2 141.3 1.0
CG A:GLU389 4.3 141.3 1.0
CG A:HIS365 4.3 142.5 1.0
ND1 A:HIS361 4.4 149.9 1.0
CG A:HIS361 4.4 149.9 1.0
ND1 A:HIS365 4.4 142.5 1.0
HA3 A:GLY392 4.7 145.3 1.0
CA A:GLU389 5.0 141.3 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: Sat Apr 8 01:51:33 2023

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