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Zinc in PDB 2xy9: Human Angiotensin Converting Enzyme in Complex with Phosphinic Tripeptide

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

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

Protein crystallography data

The structure of Human Angiotensin Converting Enzyme in Complex with Phosphinic Tripeptide, PDB code: 2xy9 was solved by M.Akif, S.L.Schwager, C.S.Anthony, B.Czarny, F.Beau, V.Dive, E.D.Sturrock, K.R.Acharya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.65 / 1.97
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 58.730, 86.094, 134.815, 90.00, 90.00, 90.00
R / Rfree (%) 19.889 / 23.18

Other elements in 2xy9:

The structure of Human Angiotensin Converting Enzyme in Complex with Phosphinic Tripeptide 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 Phosphinic Tripeptide (pdb code 2xy9). 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 Phosphinic Tripeptide, PDB code: 2xy9:

Zinc binding site 1 out of 1 in 2xy9

Go back to Zinc Binding Sites List in 2xy9
Zinc binding site 1 out of 1 in the Human Angiotensin Converting Enzyme in Complex with Phosphinic Tripeptide


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 Phosphinic Tripeptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1628

b:14.6
occ:1.00
 OE1 A:GLU411 2.0 10.2 1.0
NE2 A:HIS383 2.0 14.0 1.0
NE2 A:HIS387 2.0 14.8 1.0
OAG A:3ES1635 2.0 9.7 1.0
OAD A:3ES1635 2.7 12.1 1.0
PBY A:3ES1635 2.9 11.5 1.0
CD A:GLU411 2.9 10.8 1.0
CE1 A:HIS387 2.9 14.0 1.0
CD2 A:HIS383 3.0 14.0 1.0
CE1 A:HIS383 3.0 14.7 1.0
CD2 A:HIS387 3.1 14.6 1.0
OE2 A:GLU411 3.2 11.6 1.0
NBI A:3ES1635 3.8 12.1 1.0
CBC A:3ES1635 4.0 14.4 1.0
CBX A:3ES1635 4.0 12.0 1.0
CBM A:3ES1635 4.1 12.7 1.0
ND1 A:HIS387 4.1 14.6 1.0
ND1 A:HIS383 4.1 13.3 1.0
CG A:HIS383 4.1 13.5 1.0
CG A:HIS387 4.2 14.7 1.0
OE2 A:GLU384 4.2 16.4 1.0
CBF A:3ES1635 4.2 11.9 1.0
CG A:GLU411 4.3 10.9 1.0
OBJ A:3ES1635 4.5 12.8 1.0
CE1 A:TYR523 4.5 10.3 1.0
OAB A:3ES1635 4.5 12.7 1.0
CA A:GLU411 4.5 11.4 1.0
CB A:GLU411 4.6 11.3 1.0
O A:HOH2321 4.6 11.0 1.0
CBV A:3ES1635 4.6 13.3 1.0
CD A:GLU384 4.9 15.6 1.0
OH A:TYR523 4.9 11.4 1.0
OE1 A:GLU384 4.9 16.4 1.0

Reference:

M.Akif, S.L.Schwager, C.S.Anthony, B.Czarny, F.Beau, V.Dive, E.D.Sturrock, K.R.Acharya. Novel Mechanism of Inhibition of Human Angiotensin- I-Converting Enzyme (Ace) By A Highly Specific Phosphinic Tripeptide. Biochem.J. V. 436 53 2011.
ISSN: ISSN 0264-6021
PubMed: 21352096
DOI: 10.1042/BJ20102123
Page generated: Thu Oct 17 05:35:14 2024

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