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Zinc in PDB 4ca8: Drosophila Angiotensin Converting Enzyme (Ance) in Complex with A Phosphinic Tripeptide Fii

Enzymatic activity of Drosophila Angiotensin Converting Enzyme (Ance) in Complex with A Phosphinic Tripeptide Fii

All present enzymatic activity of Drosophila Angiotensin Converting Enzyme (Ance) in Complex with A Phosphinic Tripeptide Fii:
3.4.15.1;

Protein crystallography data

The structure of Drosophila Angiotensin Converting Enzyme (Ance) in Complex with A Phosphinic Tripeptide Fii, PDB code: 4ca8 was solved by G.Masuyer, M.Akif, B.Czarny, F.Beau, S.L.U.Schwager, E.D.Sturrock, R.E.Isaac, V.Dive, K.R.Acharya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.36 / 1.99
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 172.890, 172.890, 100.480, 90.00, 90.00, 120.00
R / Rfree (%) 19.35 / 21.64

Zinc Binding Sites:

The binding sites of Zinc atom in the Drosophila Angiotensin Converting Enzyme (Ance) in Complex with A Phosphinic Tripeptide Fii (pdb code 4ca8). 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 Drosophila Angiotensin Converting Enzyme (Ance) in Complex with A Phosphinic Tripeptide Fii, PDB code: 4ca8:

Zinc binding site 1 out of 1 in 4ca8

Go back to Zinc Binding Sites List in 4ca8
Zinc binding site 1 out of 1 in the Drosophila Angiotensin Converting Enzyme (Ance) in Complex with A Phosphinic Tripeptide Fii


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Drosophila Angiotensin Converting Enzyme (Ance) in Complex with A Phosphinic Tripeptide Fii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1620

b:24.2
occ:1.00
 NE2 A:HIS367 2.0 24.5 1.0
OE1 A:GLU395 2.1 24.0 1.0
NE2 A:HIS371 2.1 25.4 1.0
OAD A:3ES1615 2.3 24.9 1.0
OAG A:3ES1615 2.4 26.4 1.0
PBY A:3ES1615 2.6 23.8 1.0
CE1 A:HIS367 3.0 25.1 1.0
CD A:GLU395 3.0 23.4 1.0
CE1 A:HIS371 3.0 25.0 1.0
CD2 A:HIS367 3.1 24.8 1.0
CD2 A:HIS371 3.2 25.4 1.0
OE2 A:GLU395 3.3 23.5 1.0
NBI A:3ES1615 3.7 26.8 1.0
CBX A:3ES1615 3.8 26.1 1.0
CBC A:3ES1615 4.1 32.0 1.0
ND1 A:HIS367 4.1 25.0 1.0
ND1 A:HIS371 4.1 25.2 1.0
CG A:HIS367 4.2 24.8 1.0
O A:HOH2269 4.2 20.4 1.0
CG A:HIS371 4.2 25.4 1.0
OH A:TYR507 4.3 19.5 1.0
CE1 A:TYR507 4.3 18.7 1.0
CBF A:3ES1615 4.3 26.2 1.0
CBM A:3ES1615 4.3 29.3 1.0
CG A:GLU395 4.4 23.3 1.0
CBB A:3ES1615 4.6 30.8 1.0
CA A:GLU395 4.6 23.4 1.0
OE2 A:GLU368 4.6 27.6 1.0
CBV A:3ES1615 4.7 27.9 1.0
CB A:GLU395 4.7 23.2 1.0
CZ A:TYR507 4.8 18.9 1.0
OE1 A:GLU368 4.8 27.7 1.0
CBE A:3ES1615 4.9 26.6 1.0
OAB A:3ES1615 4.9 31.3 1.0
CBN A:3ES1615 5.0 27.3 1.0
OBJ A:3ES1615 5.0 31.2 1.0

Reference:

G.Masuyer, M.Akif, B.Czarny, F.Beau, S.L.Schwager, E.D.Sturrock, R.E.Isaac, V.Dive, K.R.Acharya. Crystal Structures of Highly Specific Phosphinic Tripeptide Enantiomers in Complex with the Angiotensin-I Converting Enzyme. Febs J. V. 281 943 2014.
ISSN: ISSN 1742-464X
PubMed: 24289879
DOI: 10.1111/FEBS.12660
Page generated: Wed Dec 16 05:08:14 2020

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