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Zinc in PDB 9gbo: Human Angiotensin-1 Converting Enzyme C-Domain in Complex with A Diprolyl Inhibitor- SG16

Enzymatic activity of Human Angiotensin-1 Converting Enzyme C-Domain in Complex with A Diprolyl Inhibitor- SG16

All present enzymatic activity of Human Angiotensin-1 Converting Enzyme C-Domain in Complex with A Diprolyl Inhibitor- SG16:
3.4.15.1;

Protein crystallography data

The structure of Human Angiotensin-1 Converting Enzyme C-Domain in Complex with A Diprolyl Inhibitor- SG16, PDB code: 9gbo was solved by K.S.Gregory, 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) 67.62 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.781, 84.915, 135.065, 90, 90, 90
R / Rfree (%) 19.6 / 25.5

Other elements in 9gbo:

The structure of Human Angiotensin-1 Converting Enzyme C-Domain in Complex with A Diprolyl Inhibitor- SG16 also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Angiotensin-1 Converting Enzyme C-Domain in Complex with A Diprolyl Inhibitor- SG16 (pdb code 9gbo). 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 Human Angiotensin-1 Converting Enzyme C-Domain in Complex with A Diprolyl Inhibitor- SG16, PDB code: 9gbo:

Zinc binding site 1 out of 1 in 9gbo

Go back to Zinc Binding Sites List in 9gbo
Zinc binding site 1 out of 1 in the Human Angiotensin-1 Converting Enzyme C-Domain in Complex with A Diprolyl Inhibitor- SG16


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Angiotensin-1 Converting Enzyme C-Domain in Complex with A Diprolyl Inhibitor- SG16 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:25.2
occ:1.00
 NE2 A:HIS387 1.9 25.4 1.0
OE1 A:GLU411 2.0 21.7 1.0
NE2 A:HIS383 2.0 25.5 1.0
O07 A:BJ2705 2.0 44.3 1.0
C05 A:BJ2705 2.6 41.1 1.0
O06 A:BJ2705 2.7 39.6 1.0
CE1 A:HIS387 2.8 23.0 1.0
CD A:GLU411 2.9 22.6 1.0
CE1 A:HIS383 2.9 27.7 1.0
CD2 A:HIS383 3.0 23.4 1.0
CD2 A:HIS387 3.0 27.2 1.0
OE2 A:GLU411 3.2 23.1 1.0
ND1 A:HIS387 4.0 25.7 1.0
ND1 A:HIS383 4.0 25.6 1.0
CG A:HIS383 4.1 25.4 1.0
C04 A:BJ2705 4.1 43.3 1.0
CG A:HIS387 4.1 25.1 1.0
CE1 A:TYR523 4.3 24.2 1.0
CG A:GLU411 4.3 20.7 1.0
O A:HOH976 4.4 30.3 1.0
OH A:TYR523 4.4 29.3 1.0
O14 A:BJ2705 4.5 28.0 1.0
CA A:GLU411 4.5 25.9 1.0
OE2 A:GLU384 4.7 26.4 1.0
CB A:GLU411 4.7 21.4 1.0
C02 A:BJ2705 4.7 42.5 1.0
C13 A:BJ2705 4.7 34.5 1.0
C17 A:BJ2705 4.8 38.5 1.0
N12 A:BJ2705 4.8 32.4 1.0
OE1 A:GLU384 4.9 34.7 1.0
CZ A:TYR523 4.9 23.0 1.0
C24 A:BJ2705 4.9 39.0 1.0
N03 A:BJ2705 4.9 58.9 1.0
C08 A:BJ2705 5.0 38.5 1.0

Reference:

K.S.Gregory, G.E.Cozier, S.Fienberg, K.Chibale, E.D.Sturrock, K.R.Acharya. Molecular Basis of Human Angiotensin-1 Converting Enzyme Inhibition By A Series of Diprolyl-Derived Compounds. Febs J. 2025.
ISSN: ISSN 1742-464X
PubMed: 39763019
DOI: 10.1111/FEBS.17384
Page generated: Sun Feb 9 01:21:35 2025

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