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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

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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

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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

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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

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