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Zinc in PDB 4ca7: Drosophila Angiotensin Converting Enzyme (Ance) in Complex with A Phosphinic Tripeptide Fi

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

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

Protein crystallography data

The structure of Drosophila Angiotensin Converting Enzyme (Ance) in Complex with A Phosphinic Tripeptide Fi, PDB code: 4ca7 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) 28.88 / 1.82
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 173.743, 173.743, 102.178, 90.00, 90.00, 120.00
R / Rfree (%) 17.605 / 19.402

Zinc Binding Sites:

The binding sites of Zinc atom in the Drosophila Angiotensin Converting Enzyme (Ance) in Complex with A Phosphinic Tripeptide Fi (pdb code 4ca7). 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 Fi, PDB code: 4ca7:

Zinc binding site 1 out of 1 in 4ca7

Go back to Zinc Binding Sites List in 4ca7
Zinc binding site 1 out of 1 in the Drosophila Angiotensin Converting Enzyme (Ance) in Complex with A Phosphinic Tripeptide Fi


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 Fi within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1616

b:24.1
occ:1.00
 OE1 A:GLU395 2.1 22.5 1.0
NE2 A:HIS367 2.1 22.7 1.0
NE2 A:HIS371 2.1 23.0 1.0
OAD A:3EF1715 2.2 22.3 1.0
OAG A:3EF1715 2.4 20.9 1.0
PBY A:3EF1715 2.7 22.6 1.0
CE1 A:HIS371 3.0 22.2 1.0
CE1 A:HIS367 3.0 22.8 1.0
CD A:GLU395 3.0 21.7 1.0
CD2 A:HIS367 3.1 22.6 1.0
CD2 A:HIS371 3.2 22.2 1.0
OE2 A:GLU395 3.3 21.7 1.0
NBI A:3EF1715 3.7 22.4 1.0
CBX A:3EF1715 4.0 22.2 1.0
ND1 A:HIS367 4.1 22.9 1.0
ND1 A:HIS371 4.2 22.1 1.0
CG A:HIS367 4.2 22.7 1.0
CE1 A:TYR507 4.2 20.6 1.0
CBF A:3EF1715 4.2 21.6 1.0
OH A:TYR507 4.2 22.0 1.0
O A:HOH2429 4.2 21.1 1.0
CG A:HIS371 4.3 22.5 1.0
CBM A:3EF1715 4.3 24.6 1.0
CBV A:3EF1715 4.4 23.8 1.0
CG A:GLU395 4.4 21.8 1.0
CA A:GLU395 4.6 22.1 1.0
CB A:GLU395 4.7 21.7 1.0
OBJ A:3EF1715 4.7 24.7 1.0
OE1 A:GLU368 4.7 24.6 1.0
CZ A:TYR507 4.7 20.7 1.0
OE2 A:GLU368 4.8 25.3 1.0
CBN A:3EF1715 4.8 23.6 1.0
OAB A:3EF1715 4.9 25.1 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: Sat Oct 26 20:42:33 2024

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