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Zinc in PDB 4aph: Human Angiotensin-Converting Enzyme in Complex with Angiotensin-II

Enzymatic activity of Human Angiotensin-Converting Enzyme in Complex with Angiotensin-II

All present enzymatic activity of Human Angiotensin-Converting Enzyme in Complex with Angiotensin-II:
3.4.15.1;

Protein crystallography data

The structure of Human Angiotensin-Converting Enzyme in Complex with Angiotensin-II, PDB code: 4aph was solved by G.Masuyer, S.L.U.Schwager, E.D.Sturrock, R.E.Isaac, K.R.Acharya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 71.57 / 1.99
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.500, 84.660, 133.970, 90.00, 90.00, 90.00
R / Rfree (%) 19.406 / 24.026

Other elements in 4aph:

The structure of Human Angiotensin-Converting Enzyme in Complex with Angiotensin-II also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Angiotensin-Converting Enzyme in Complex with Angiotensin-II (pdb code 4aph). 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-Converting Enzyme in Complex with Angiotensin-II, PDB code: 4aph:

Zinc binding site 1 out of 1 in 4aph

Go back to Zinc Binding Sites List in 4aph
Zinc binding site 1 out of 1 in the Human Angiotensin-Converting Enzyme in Complex with Angiotensin-II


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Angiotensin-Converting Enzyme in Complex with Angiotensin-II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1627

b:30.8
occ:1.00
 O P:TYR4 1.9 24.2 0.5
NE2 A:HIS383 2.0 15.3 1.0
OE1 A:GLU411 2.0 14.1 1.0
NE2 A:HIS387 2.1 14.2 1.0
O P:ILE5 2.2 20.9 0.5
CE1 A:HIS383 2.7 15.5 1.0
C P:TYR4 2.9 24.5 0.5
CE1 A:HIS387 3.0 14.3 1.0
CD A:GLU411 3.0 13.0 1.0
CD2 A:HIS383 3.0 15.2 1.0
CD2 A:HIS387 3.1 14.8 1.0
C P:ILE5 3.2 21.1 0.5
OE2 A:GLU411 3.3 13.4 1.0
CA P:ILE5 3.6 25.8 0.5
N P:ILE5 3.6 25.2 0.5
ND1 A:HIS383 3.8 14.7 1.0
N P:HIS6 3.9 21.6 0.5
CA P:HIS6 4.0 21.8 0.5
CG A:HIS383 4.0 15.2 1.0
CA P:TYR4 4.0 24.0 0.5
N P:TYR4 4.0 24.1 0.5
N P:ILE5 4.1 20.3 0.5
ND1 A:HIS387 4.1 14.4 1.0
CA P:ILE5 4.2 20.8 0.5
CG A:HIS387 4.2 14.7 1.0
OE2 A:GLU384 4.2 16.2 1.0
CG A:GLU411 4.3 12.3 1.0
CE1 A:TYR523 4.3 11.0 1.0
CA A:GLU411 4.4 12.1 1.0
O A:HOH2217 4.4 19.7 1.0
CB P:ILE5 4.5 25.9 0.5
C P:VAL3 4.5 24.2 0.5
CB A:GLU411 4.6 11.9 1.0
CG2 P:ILE5 4.6 26.1 0.5
C P:TYR4 4.7 20.0 0.5
O P:VAL3 4.7 24.0 0.5
CG1 P:VAL3 4.8 24.6 0.5
C P:ILE5 4.8 26.1 0.5
OH A:TYR523 4.8 12.4 1.0
CD A:GLU384 4.8 16.9 1.0
OE1 A:GLU384 4.9 18.7 1.0
C P:HIS6 4.9 21.8 0.5
O A:HIS383 5.0 14.8 1.0
CB P:TYR4 5.0 19.6 0.5

Reference:

G.Masuyer, S.L.U.Schwager, E.D.Sturrock, R.E.Isaac, K.R.Acharya. Molecular Recognition and Regulation of Human Angiotensin-I Converting Enzyme (Ace) Activity By Natural Inhibitory Peptides. Sci.Rep. V. 2 717 2012.
ISSN: ISSN 2045-2322
PubMed: 23056909
DOI: 10.1038/SREP00717
Page generated: Sat Oct 26 19:19:19 2024

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