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Zinc in PDB 5amc: Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta Fluorogenic Fragment 4-10

Enzymatic activity of Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta Fluorogenic Fragment 4-10

All present enzymatic activity of Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta Fluorogenic Fragment 4-10:
3.4.15.1;

Protein crystallography data

The structure of Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta Fluorogenic Fragment 4-10, PDB code: 5amc was solved by G.Masuyer, K.M.Larmuth, R.G.Douglas, 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) 74.53 / 1.65
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 73.029, 76.470, 83.158, 88.78, 64.25, 75.64
R / Rfree (%) 20.772 / 24.169

Other elements in 5amc:

The structure of Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta Fluorogenic Fragment 4-10 also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta Fluorogenic Fragment 4-10 (pdb code 5amc). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta Fluorogenic Fragment 4-10, PDB code: 5amc:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 5amc

Go back to Zinc Binding Sites List in 5amc
Zinc binding site 1 out of 2 in the Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta Fluorogenic Fragment 4-10


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta Fluorogenic Fragment 4-10 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1001

b:19.6
occ:1.00
 OE1 A:GLU389 2.1 18.8 1.0
NE2 A:HIS365 2.1 17.5 1.0
O A:HOH2339 2.1 18.8 1.0
NE2 A:HIS361 2.2 19.0 1.0
O A:HOH2340 2.2 27.6 1.0
CE1 A:HIS365 3.0 17.8 1.0
CD A:GLU389 3.0 20.2 1.0
CD2 A:HIS361 3.1 18.4 1.0
CD2 A:HIS365 3.1 17.6 1.0
CE1 A:HIS361 3.1 18.1 1.0
OE2 A:GLU389 3.3 20.1 1.0
CA A:GLY906 4.0 43.2 1.0
N A:GLY906 4.1 44.8 1.0
ND1 A:HIS365 4.1 17.7 1.0
ND1 A:HIS361 4.2 17.7 1.0
O A:HOH2321 4.2 35.1 1.0
CG A:HIS365 4.2 17.6 1.0
CG A:HIS361 4.2 17.2 1.0
CE1 A:TYR501 4.3 19.0 1.0
OH A:TYR501 4.4 18.7 1.0
CG A:GLU389 4.4 19.7 1.0
OE2 A:GLU362 4.4 24.3 1.0
O A:HOH2350 4.5 25.9 1.0
C A:GLY906 4.5 42.8 1.0
OE1 A:GLU362 4.6 23.9 1.0
CA A:GLU389 4.7 18.8 1.0
CB A:GLU389 4.8 19.7 1.0
CD A:GLU362 4.8 22.8 1.0
CZ A:TYR501 4.8 19.0 1.0
O A:GLY906 4.9 44.8 1.0
N A:NIY907 5.0 40.2 1.0

Zinc binding site 2 out of 2 in 5amc

Go back to Zinc Binding Sites List in 5amc
Zinc binding site 2 out of 2 in the Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta Fluorogenic Fragment 4-10


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta Fluorogenic Fragment 4-10 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1001

b:20.1
occ:1.00
 OE1 B:GLU389 1.9 22.5 1.0
O B:HOH2279 1.9 33.9 1.0
NE2 B:HIS365 2.1 21.6 1.0
NE2 B:HIS361 2.1 19.5 1.0
O B:HOH2280 2.1 23.8 1.0
CD B:GLU389 2.9 22.9 1.0
CE1 B:HIS365 3.0 23.0 1.0
CE1 B:HIS361 3.1 19.1 1.0
CD2 B:HIS361 3.1 19.0 1.0
OE2 B:GLU389 3.2 22.5 1.0
CD2 B:HIS365 3.2 21.2 1.0
CA B:GLY906 4.0 45.9 1.0
O B:HOH2255 4.1 32.9 1.0
ND1 B:HIS361 4.1 18.9 1.0
ND1 B:HIS365 4.2 23.0 1.0
CG B:HIS361 4.2 17.6 1.0
CG B:GLU389 4.2 23.0 1.0
CG B:HIS365 4.3 21.4 1.0
CE1 B:TYR501 4.3 19.2 1.0
OE2 B:GLU362 4.3 25.7 1.0
OH B:TYR501 4.4 19.0 1.0
O B:HOH2287 4.5 28.3 1.0
O4 B:PEG1622 4.6 56.5 1.0
CA B:GLU389 4.6 22.2 1.0
C B:GLY906 4.6 44.0 1.0
CB B:GLU389 4.6 23.2 1.0
OE1 B:GLU362 4.7 26.1 1.0
CZ B:TYR501 4.8 18.9 1.0
CD B:GLU362 4.8 23.7 1.0

Reference:

K.M.Larmuth, G.Masuyer, R.G.Douglas, E.D.Sturrock, K.R.Acharya. The Kinetic and Structural Characterisation of Amyloid-Beta Metabolism By Human Angiotensin-1- Converting Enzyme (Ace) Febs J. V. 283 1060 2016.
ISSN: ISSN 1742-464X
PubMed: 26748546
DOI: 10.1111/FEBS.13647
Page generated: Sun Oct 27 13:06:03 2024

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