Atomistry » Zinc » PDB 5aeh-5ami » 5am8
Atomistry »
  Zinc »
    PDB 5aeh-5ami »
      5am8 »

Zinc in PDB 5am8: Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 4-10

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

All present enzymatic activity of Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 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 4-10, PDB code: 5am8 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) 113.78 / 1.90
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 73.449, 101.760, 114.361, 85.23, 86.07, 81.45
R / Rfree (%) 18.543 / 22.382

Other elements in 5am8:

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

Chlorine (Cl) 4 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 4-10 (pdb code 5am8). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 4-10, PDB code: 5am8:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 5am8

Go back to Zinc Binding Sites List in 5am8
Zinc binding site 1 out of 4 in the Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 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 4-10 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1001

b:19.4
occ:1.00
 OE1 A:GLU389 1.9 18.1 1.0
O A:HOH2289 2.0 16.3 1.0
NE2 A:HIS361 2.0 16.9 1.0
NE2 A:HIS365 2.1 19.6 1.0
O A:HOH2288 2.4 29.1 1.0
CE1 A:HIS361 2.9 17.5 1.0
CD A:GLU389 2.9 18.7 1.0
CE1 A:HIS365 3.0 19.6 1.0
CD2 A:HIS361 3.1 17.6 1.0
CD2 A:HIS365 3.1 19.8 1.0
OE2 A:GLU389 3.3 18.2 1.0
ND1 A:HIS361 4.0 17.9 1.0
N P:ASP7 4.1 25.3 1.0
ND1 A:HIS365 4.1 19.5 1.0
CG A:HIS361 4.1 17.1 1.0
CE1 A:TYR501 4.1 16.2 1.0
O A:HOH2266 4.2 23.2 1.0
CG A:HIS365 4.2 19.2 1.0
CA P:ASP7 4.3 25.8 1.0
CG A:GLU389 4.3 19.3 1.0
O A:HOH2298 4.3 18.5 1.0
OH A:TYR501 4.3 17.0 1.0
OE1 A:GLU362 4.4 21.1 1.0
OE2 A:GLU362 4.6 20.9 1.0
CA A:GLU389 4.6 19.9 1.0
CB A:GLU389 4.7 19.4 1.0
CZ A:TYR501 4.7 16.4 1.0
C P:ASP7 4.8 23.1 1.0
O A:HOH2265 4.8 28.7 1.0
CD A:GLU362 4.9 20.3 1.0

Zinc binding site 2 out of 4 in 5am8

Go back to Zinc Binding Sites List in 5am8
Zinc binding site 2 out of 4 in the Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 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 4-10 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1001

b:16.5
occ:1.00
 OE1 B:GLU389 1.9 14.1 1.0
NE2 B:HIS361 2.1 14.5 1.0
O B:HOH2324 2.1 15.6 1.0
NE2 B:HIS365 2.1 16.5 1.0
O B:HOH2323 2.5 29.2 1.0
CD B:GLU389 2.9 14.8 1.0
CE1 B:HIS365 2.9 16.0 1.0
CD2 B:HIS361 3.0 14.5 1.0
CE1 B:HIS361 3.0 14.2 1.0
CD2 B:HIS365 3.2 16.1 1.0
OE2 B:GLU389 3.2 14.7 1.0
N Q:ASP7 3.8 24.8 1.0
O B:HOH2300 4.0 27.1 1.0
ND1 B:HIS365 4.1 16.6 1.0
ND1 B:HIS361 4.1 14.7 1.0
CE1 B:TYR501 4.1 14.8 1.0
CG B:HIS361 4.1 14.3 1.0
CA Q:ASP7 4.2 24.4 1.0
CG B:HIS365 4.2 15.8 1.0
OH B:TYR501 4.3 15.0 1.0
CG B:GLU389 4.3 15.0 1.0
O B:HOH2334 4.5 19.4 1.0
OE1 B:GLU362 4.5 17.6 1.0
OE2 B:GLU362 4.5 17.2 1.0
CA B:GLU389 4.6 15.5 1.0
CZ B:TYR501 4.7 14.9 1.0
O B:HOH2299 4.7 34.7 1.0
CB B:GLU389 4.7 15.3 1.0
C Q:ASP7 4.7 20.8 1.0
CD B:GLU362 4.8 16.8 1.0
C4 B:PEG1205 4.9 51.8 1.0

Zinc binding site 3 out of 4 in 5am8

Go back to Zinc Binding Sites List in 5am8
Zinc binding site 3 out of 4 in the Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 4-10


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 4-10 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn1001

b:15.8
occ:1.00
 OE1 C:GLU389 1.9 14.0 1.0
NE2 C:HIS365 2.0 12.7 1.0
O C:HOH2362 2.0 10.9 1.0
NE2 C:HIS361 2.1 14.2 1.0
O C:HOH2361 2.4 29.4 1.0
CD C:GLU389 2.9 14.1 1.0
CE1 C:HIS365 2.9 13.2 1.0
CD2 C:HIS361 3.0 14.0 1.0
CE1 C:HIS361 3.1 14.4 1.0
CD2 C:HIS365 3.1 13.1 1.0
OE2 C:GLU389 3.2 14.1 1.0
N R:ASP7 3.9 26.5 1.0
ND1 C:HIS365 4.1 13.2 1.0
CE1 C:TYR501 4.1 13.1 1.0
ND1 C:HIS361 4.1 13.8 1.0
CG C:HIS361 4.1 13.6 1.0
OH C:TYR501 4.2 12.9 1.0
CG C:HIS365 4.2 13.3 1.0
CG C:GLU389 4.2 14.1 1.0
O C:HOH2334 4.3 30.4 1.0
CA R:ASP7 4.3 24.8 1.0
CA C:GLU389 4.5 13.9 1.0
O C:HOH2372 4.5 14.1 1.0
OE2 C:GLU362 4.6 15.0 1.0
CB C:GLU389 4.6 14.1 1.0
OE1 C:GLU362 4.6 15.9 1.0
CZ C:TYR501 4.6 13.2 1.0
C R:ASP7 4.8 21.5 1.0
C3 C:PEG1203 4.9 44.4 1.0
CD C:GLU362 4.9 15.2 1.0
O C:HOH2333 4.9 33.3 1.0

Zinc binding site 4 out of 4 in 5am8

Go back to Zinc Binding Sites List in 5am8
Zinc binding site 4 out of 4 in the Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 4-10


Mono view


Stereo pair view

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

b:15.3
occ:1.00
 OE1 D:GLU389 1.9 16.2 1.0
NE2 D:HIS361 2.0 14.8 1.0
NE2 D:HIS365 2.0 15.9 1.0
O D:HOH2335 2.0 11.4 1.0
O D:HOH2334 2.2 34.5 1.0
CD D:GLU389 2.9 15.3 1.0
CE1 D:HIS365 3.0 15.5 1.0
CE1 D:HIS361 3.0 14.2 1.0
CD2 D:HIS361 3.0 14.2 1.0
CD2 D:HIS365 3.1 16.0 1.0
OE2 D:GLU389 3.2 15.3 1.0
N S:ASP7 3.9 24.2 1.0
O D:HOH2313 4.0 28.8 1.0
ND1 D:HIS361 4.1 14.4 1.0
ND1 D:HIS365 4.1 16.1 1.0
CG D:HIS361 4.1 14.1 1.0
CE1 D:TYR501 4.2 12.9 1.0
CG D:HIS365 4.2 15.5 1.0
CG D:GLU389 4.3 15.4 1.0
CA S:ASP7 4.3 24.4 1.0
OH D:TYR501 4.3 13.6 1.0
O D:HOH2346 4.4 15.7 1.0
OE1 D:GLU362 4.5 16.7 1.0
CA D:GLU389 4.6 15.0 1.0
OE2 D:GLU362 4.6 15.5 1.0
O D:HOH2312 4.7 39.0 1.0
CB D:GLU389 4.7 14.8 1.0
CZ D:TYR501 4.7 12.9 1.0
C S:ASP7 4.8 21.6 1.0
C3 D:PEG1204 4.8 49.5 1.0
CD D:GLU362 4.9 16.0 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 13:04:58 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy