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Zinc in PDB 5ama: Crystal Structure of the Angiotensin-1 Converting Enzyme N-Domain in Complex with Amyloid-Beta 1-16

Enzymatic activity of Crystal Structure of the Angiotensin-1 Converting Enzyme N-Domain in Complex with Amyloid-Beta 1-16

All present enzymatic activity of Crystal Structure of the Angiotensin-1 Converting Enzyme N-Domain in Complex with Amyloid-Beta 1-16:
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 1-16, PDB code: 5ama 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) 113.48 / 1.80
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 73.340, 101.730, 114.140, 85.09, 85.62, 81.30
R / Rfree (%) 18.7 / 21.8

Other elements in 5ama:

The structure of Crystal Structure of the Angiotensin-1 Converting Enzyme N-Domain in Complex with Amyloid-Beta 1-16 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 1-16 (pdb code 5ama). 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 1-16, PDB code: 5ama:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 5ama

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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 1-16


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 1-16 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1001

b:18.8
occ:1.00
 OE1 A:GLU389 2.0 18.7 1.0
NE2 A:HIS361 2.1 17.6 1.0
NE2 A:HIS365 2.1 17.4 1.0
O A:HOH2320 2.2 22.5 1.0
O A:HOH2319 2.2 39.9 1.0
CE1 A:HIS365 2.9 17.6 1.0
CD A:GLU389 3.0 18.7 1.0
CD2 A:HIS361 3.0 17.4 1.0
CE1 A:HIS361 3.0 17.5 1.0
CD2 A:HIS365 3.2 17.4 1.0
OE2 A:GLU389 3.3 17.9 1.0
N A:ASP907 4.0 26.5 1.0
ND1 A:HIS365 4.1 17.6 1.0
ND1 A:HIS361 4.1 17.7 1.0
CG A:HIS361 4.1 17.4 1.0
CE1 A:TYR501 4.2 17.3 1.0
O A:HOH2424 4.2 39.5 1.0
CG A:HIS365 4.3 17.2 1.0
CA A:ASP907 4.3 26.8 1.0
O A:HOH2299 4.3 26.8 1.0
CG A:GLU389 4.3 18.5 1.0
OH A:TYR501 4.4 17.7 1.0
O A:HOH2328 4.5 21.7 1.0
OE1 A:GLU362 4.5 21.2 1.0
OE2 A:GLU362 4.6 19.9 1.0
CA A:GLU389 4.6 18.9 1.0
CB A:GLU389 4.7 18.9 1.0
CZ A:TYR501 4.8 17.5 1.0
C1 A:PEG1204 4.8 40.3 1.0
C A:ASP907 4.8 24.1 1.0
O A:HOH2298 4.9 35.9 1.0
CD A:GLU362 4.9 20.1 1.0

Zinc binding site 2 out of 4 in 5ama

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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 1-16


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 1-16 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1001

b:17.6
occ:1.00
 OE1 B:GLU389 2.0 14.6 1.0
NE2 B:HIS365 2.1 16.1 1.0
NE2 B:HIS361 2.1 15.5 1.0
O B:HOH2336 2.2 19.8 1.0
O B:HOH2335 2.3 30.6 1.0
CE1 B:HIS365 2.9 15.9 1.0
CD B:GLU389 2.9 14.9 1.0
CE1 B:HIS361 3.0 15.2 1.0
CD2 B:HIS361 3.0 15.3 1.0
CD2 B:HIS365 3.2 15.8 1.0
OE2 B:GLU389 3.2 15.1 1.0
N B:ASP907 3.9 27.6 1.0
ND1 B:HIS365 4.1 16.0 1.0
ND1 B:HIS361 4.1 15.3 1.0
CG B:HIS361 4.1 15.1 1.0
CE1 B:TYR501 4.2 16.0 1.0
O B:HOH2313 4.2 34.1 1.0
CG B:HIS365 4.2 15.4 1.0
CG B:GLU389 4.3 14.8 1.0
CA B:ASP907 4.4 27.7 1.0
OH B:TYR501 4.4 16.6 1.0
O B:HOH2348 4.4 20.3 1.0
OE1 B:GLU362 4.5 18.0 1.0
CA B:GLU389 4.6 15.5 1.0
OE2 B:GLU362 4.6 18.5 1.0
C14 B:P6G1204 4.7 49.4 1.0
CB B:GLU389 4.7 15.2 1.0
O B:HOH2312 4.7 45.4 1.0
CZ B:TYR501 4.8 16.0 1.0
C B:ASP907 4.8 24.8 1.0
CD B:GLU362 4.8 17.8 1.0

Zinc binding site 3 out of 4 in 5ama

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Zinc binding site 3 out of 4 in the Crystal Structure of the Angiotensin-1 Converting Enzyme N-Domain in Complex with Amyloid-Beta 1-16


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 1-16 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn1001

b:15.6
occ:1.00
 OE1 C:GLU389 2.0 13.6 1.0
NE2 C:HIS361 2.1 14.4 1.0
NE2 C:HIS365 2.1 13.1 1.0
O C:HOH2366 2.1 17.1 1.0
O C:HOH2365 2.4 28.5 1.0
CD C:GLU389 2.9 13.5 1.0
CE1 C:HIS365 2.9 13.2 1.0
CE1 C:HIS361 3.0 14.4 1.0
CD2 C:HIS361 3.1 14.5 1.0
OE2 C:GLU389 3.1 14.0 1.0
CD2 C:HIS365 3.2 13.3 1.0
CA C:ASP907 4.0 23.1 1.0
ND1 C:HIS365 4.1 13.2 1.0
ND1 C:HIS361 4.1 14.2 1.0
CE1 C:TYR501 4.1 13.7 1.0
CG C:HIS361 4.2 13.8 1.0
CG C:HIS365 4.3 13.1 1.0
CG C:GLU389 4.3 13.5 1.0
O C:HOH2342 4.3 32.0 1.0
N C:ASP907 4.4 23.1 1.0
O C:HOH2377 4.4 16.7 1.0
OH C:TYR501 4.4 14.4 1.0
CA C:GLU389 4.5 13.4 1.0
OE2 C:GLU362 4.6 16.3 1.0
CB C:GLU389 4.6 13.5 1.0
OE1 C:GLU362 4.6 16.2 1.0
CZ C:TYR501 4.8 14.0 1.0
C C:ASP907 4.8 21.0 1.0
CD C:GLU362 4.9 15.6 1.0
O C:HOH2341 4.9 29.8 1.0
CB C:ASP907 5.0 25.3 1.0

Zinc binding site 4 out of 4 in 5ama

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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 1-16


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 1-16 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn1001

b:17.1
occ:1.00
 OE1 D:GLU389 1.9 15.5 1.0
NE2 D:HIS365 2.1 15.6 1.0
NE2 D:HIS361 2.1 16.6 1.0
O D:HOH2323 2.2 25.0 1.0
O D:HOH2324 2.3 19.6 1.0
CE1 D:HIS365 2.9 15.4 1.0
CD D:GLU389 2.9 15.5 1.0
CD2 D:HIS361 3.0 16.2 1.0
CE1 D:HIS361 3.1 16.2 1.0
OE2 D:GLU389 3.1 15.9 1.0
CD2 D:HIS365 3.2 15.3 1.0
N D:ASP907 4.0 25.5 1.0
O D:HOH2304 4.0 32.3 1.0
ND1 D:HIS365 4.0 15.6 1.0
ND1 D:HIS361 4.1 16.2 1.0
CG D:HIS361 4.2 15.8 1.0
CE1 D:TYR501 4.2 14.0 1.0
CG D:HIS365 4.2 15.0 1.0
CG D:GLU389 4.3 15.5 1.0
CA D:ASP907 4.3 25.8 1.0
O D:HOH2334 4.4 18.1 1.0
OH D:TYR501 4.5 14.5 1.0
OE1 D:GLU362 4.5 18.0 1.0
CA D:GLU389 4.6 15.3 1.0
OE2 D:GLU362 4.6 17.9 1.0
CB D:GLU389 4.7 15.4 1.0
C D:ASP907 4.8 23.1 1.0
CZ D:TYR501 4.8 14.3 1.0
CD D:GLU362 4.9 17.3 1.0
C5 D:P6G1203 4.9 47.7 1.0
O D:HOH2303 4.9 36.4 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 13:06:04 2024

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