Zinc in PDB 6zpt: Crystal Structure of the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain.
Enzymatic activity of Crystal Structure of the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain.
All present enzymatic activity of Crystal Structure of the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain.:
3.4.15.1;
3.4.15.1;
Protein crystallography data
The structure of Crystal Structure of the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain., PDB code: 6zpt
was solved by
G.E.Cozier,
K.R.Acharya,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 69.05 / 2.80 |
| Space group | P 1 |
| Cell size a, b, c (Å), α, β, γ (°) | 73.650, 99.257, 127.980, 98.63, 89.63, 111.15 |
| R / Rfree (%) | 22.4 / 27.8 |
Other elements in 6zpt:
The structure of Crystal Structure of the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain. also contains other interesting chemical elements:
| Calcium | (Ca) | 4 atoms |
| Chlorine | (Cl) | 4 atoms |
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain.
(pdb code 6zpt). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain., PDB code: 6zpt:
Jump to Zinc binding site number: 1; 2; 3; 4;
In total 4 binding sites of Zinc where determined in the Crystal Structure of the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain., PDB code: 6zpt:
Jump to Zinc binding site number: 1; 2; 3; 4;
Zinc binding site 1 out of 4 in 6zpt
Go back to
Zinc Binding Sites List in 6zpt
Zinc binding site 1 out
of 4 in the Crystal Structure of the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain.
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Crystal Structure of the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain. within 5.0Å range:
|
Zinc binding site 2 out of 4 in 6zpt
Go back to
Zinc Binding Sites List in 6zpt
Zinc binding site 2 out
of 4 in the Crystal Structure of the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain.
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Crystal Structure of the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain. within 5.0Å range:
|
Zinc binding site 3 out of 4 in 6zpt
Go back to
Zinc Binding Sites List in 6zpt
Zinc binding site 3 out
of 4 in the Crystal Structure of the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain.
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Crystal Structure of the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain. within 5.0Å range:
|
Zinc binding site 4 out of 4 in 6zpt
Go back to
Zinc Binding Sites List in 6zpt
Zinc binding site 4 out
of 4 in the Crystal Structure of the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain.
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Crystal Structure of the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain. within 5.0Å range:
|
Reference:
G.E.Cozier,
L.Lubbe,
E.D.Sturrock,
K.R.Acharya.
Angiotensin-Converting Enzyme Open For Business: Structural Insights Into the Sub-Domain Dynamics. Febs J. 2020.
ISSN: ISSN 1742-464X
PubMed: 33067882
DOI: 10.1111/FEBS.15601
Page generated: Wed Dec 16 13:30:09 2020
ISSN: ISSN 1742-464X
PubMed: 33067882
DOI: 10.1111/FEBS.15601
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