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Zinc in PDB 4ca5: Human Angiotensin Converting Enzyme in Complex with A Phosphinic Tripeptide Fi

Enzymatic activity of Human Angiotensin Converting Enzyme in Complex with A Phosphinic Tripeptide Fi

All present enzymatic activity of Human Angiotensin Converting Enzyme in Complex with A Phosphinic Tripeptide Fi:
3.4.15.1;

Protein crystallography data

The structure of Human Angiotensin Converting Enzyme in Complex with A Phosphinic Tripeptide Fi, PDB code: 4ca5 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) 71.75 / 1.85
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.430, 84.980, 133.900, 90.00, 90.00, 90.00
R / Rfree (%) 18.057 / 21.344

Other elements in 4ca5:

The structure of Human Angiotensin Converting Enzyme in Complex with A Phosphinic Tripeptide Fi 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 A Phosphinic Tripeptide Fi (pdb code 4ca5). 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 A Phosphinic Tripeptide Fi, PDB code: 4ca5:

Zinc binding site 1 out of 1 in 4ca5

Go back to Zinc Binding Sites List in 4ca5
Zinc binding site 1 out of 1 in the Human Angiotensin Converting Enzyme 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 Human Angiotensin Converting Enzyme in Complex with A Phosphinic Tripeptide Fi within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1001

b:10.3
occ:1.00
 OE1 A:GLU411 2.0 9.0 1.0
NE2 A:HIS387 2.0 9.8 1.0
NE2 A:HIS383 2.1 10.7 1.0
OAD A:3EF1700 2.2 10.5 1.0
OAG A:3EF1700 2.4 11.0 1.0
PBY A:3EF1700 2.7 10.9 1.0
CD A:GLU411 2.9 8.9 1.0
CE1 A:HIS387 2.9 9.8 1.0
CD2 A:HIS383 3.0 10.4 1.0
CE1 A:HIS383 3.0 10.4 1.0
CD2 A:HIS387 3.1 10.0 1.0
OE2 A:GLU411 3.2 9.1 1.0
NBI A:3EF1700 3.8 11.2 1.0
CBX A:3EF1700 4.0 11.0 1.0
ND1 A:HIS387 4.1 9.9 1.0
ND1 A:HIS383 4.1 10.4 1.0
CBF A:3EF1700 4.1 11.6 1.0
CE1 A:TYR523 4.1 7.6 1.0
CG A:HIS383 4.2 10.4 1.0
CG A:HIS387 4.2 9.9 1.0
CBV A:3EF1700 4.2 12.2 1.0
CBM A:3EF1700 4.3 11.7 1.0
CG A:GLU411 4.3 8.7 1.0
O A:HOH2274 4.3 10.5 1.0
OH A:TYR523 4.3 7.4 1.0
CA A:GLU411 4.6 8.8 1.0
CB A:GLU411 4.7 8.8 1.0
OBJ A:3EF1700 4.7 11.8 1.0
OE1 A:GLU384 4.7 12.1 1.0
CZ A:TYR523 4.8 7.6 1.0
CBN A:3EF1700 4.8 12.0 1.0
OAB A:3EF1700 4.8 11.8 1.0
OE2 A:GLU384 4.8 11.8 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 05:08:13 2020

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