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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 2xyd:

The structure of Human Angiotenisn Converting Enzyme N-Domain 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 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 2xyd

Go back to Zinc Binding Sites List in 2xyd
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 2xyd

Go back to Zinc Binding Sites List in 2xyd
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

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 05:35:38 2024

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