Zinc in PDB 2xyd: Human Angiotenisn Converting Enzyme N-Domain in Complex with Phosphinic Tripeptide

All present enzymatic activity of Human Angiotenisn Converting Enzyme N-Domain in Complex with Phosphinic Tripeptide:
3.4.15.1;

The structure of Human Angiotenisn Converting Enzyme N-Domain in Complex with Phosphinic Tripeptide, PDB code: 2xyd 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)	40.28 / 2.15
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	72.837, 76.437, 82.954, 89.11, 64.43, 75.87
R / Rfree (%)	21.991 / 25.589

The structure of Human Angiotenisn Converting Enzyme N-Domain in Complex with Phosphinic Tripeptide also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Zinc atom in the Human Angiotenisn Converting Enzyme N-Domain in Complex with Phosphinic Tripeptide (pdb code 2xyd). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Human Angiotenisn Converting Enzyme N-Domain in Complex with Phosphinic Tripeptide, PDB code: 2xyd:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Human Angiotenisn Converting Enzyme N-Domain 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 Angiotenisn Converting Enzyme N-Domain in Complex with Phosphinic Tripeptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1620 b:25.1 occ:1.00 OE1 A:GLU389 1.9 25.1 1.0 NE2 A:HIS365 2.0 24.6 1.0 NE2 A:HIS361 2.0 28.9 1.0 OAD A:3ES1611 2.2 22.5 1.0 OAG A:3ES1611 2.3 24.6 1.0 PBY A:3ES1611 2.7 26.6 1.0 CE1 A:HIS365 2.8 25.5 1.0 CD A:GLU389 3.0 25.5 1.0 CE1 A:HIS361 3.0 27.1 1.0 CD2 A:HIS361 3.1 26.5 1.0 CD2 A:HIS365 3.2 24.9 1.0 OE2 A:GLU389 3.3 25.2 1.0 NBI A:3ES1611 3.7 27.9 1.0 CBC A:3ES1611 4.0 32.4 1.0 CBX A:3ES1611 4.0 26.0 1.0 ND1 A:HIS365 4.0 24.7 1.0 ND1 A:HIS361 4.1 26.6 1.0 CBM A:3ES1611 4.1 30.3 1.0 CE1 A:TYR501 4.1 16.8 1.0 CG A:HIS361 4.2 24.1 1.0 CG A:HIS365 4.2 24.2 1.0 CBF A:3ES1611 4.2 27.0 1.0 CG A:GLU389 4.3 24.6 1.0 OH A:TYR501 4.3 18.4 1.0 CA A:GLU389 4.6 23.9 1.0 OBJ A:3ES1611 4.6 28.2 1.0 CBV A:3ES1611 4.6 29.8 1.0 OE2 A:GLU362 4.6 31.0 1.0 CB A:GLU389 4.6 24.5 1.0 OAB A:3ES1611 4.6 28.8 1.0 CZ A:TYR501 4.8 16.0 1.0 OE1 A:GLU362 4.9 28.6 1.0 CBB A:3ES1611 4.9 32.0 1.0

Zinc binding site 2 out of 2 in the Human Angiotenisn Converting Enzyme N-Domain 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 2 of Human Angiotenisn Converting Enzyme N-Domain in Complex with Phosphinic Tripeptide within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1619 b:23.7 occ:1.00 NE2 B:HIS361 2.0 25.5 1.0 NE2 B:HIS365 2.0 27.2 1.0 OAD B:3ES1611 2.0 26.6 1.0 OE1 B:GLU389 2.1 27.6 1.0 OAG B:3ES1611 2.4 23.8 1.0 PBY B:3ES1611 2.7 28.5 1.0 CE1 B:HIS365 2.9 28.8 1.0 CD B:GLU389 2.9 27.8 1.0 CD2 B:HIS361 2.9 25.4 1.0 CE1 B:HIS361 3.0 25.0 1.0 CD2 B:HIS365 3.1 27.5 1.0 OE2 B:GLU389 3.1 27.4 1.0 NBI B:3ES1611 3.8 29.8 1.0 CBX B:3ES1611 3.9 27.9 1.0 ND1 B:HIS361 4.1 25.1 1.0 ND1 B:HIS365 4.1 27.6 1.0 CE1 B:TYR501 4.1 21.8 1.0 CG B:HIS361 4.1 24.1 1.0 CBC B:3ES1611 4.2 33.2 1.0 CG B:HIS365 4.2 28.2 1.0 CBM B:3ES1611 4.2 33.6 1.0 CBF B:3ES1611 4.2 27.9 1.0 OH B:TYR501 4.2 23.1 1.0 CBB B:3ES1611 4.2 37.3 1.0 CG B:GLU389 4.3 26.9 1.0 O B:HOH2066 4.4 30.5 1.0 CA B:GLU389 4.6 26.3 1.0 OAB B:3ES1611 4.6 32.5 1.0 OE2 B:GLU362 4.6 27.7 1.0 CBV B:3ES1611 4.6 29.0 1.0 CZ B:TYR501 4.7 21.0 1.0 CB B:GLU389 4.7 26.1 1.0 OBJ B:3ES1611 4.8 34.8 1.0

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