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Zinc in PDB 5am9: Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 10-16

Enzymatic activity of Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 10-16

All present enzymatic activity of Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 10-16:
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 10-16, PDB code: 5am9 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) 113.27 / 1.80
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 73.348, 101.800, 113.950, 85.04, 85.55, 81.88
R / Rfree (%) 19.674 / 22.907

Other elements in 5am9:

The structure of Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 10-16 also contains other interesting chemical elements:

Calcium (Ca) 2 atoms
Chlorine (Cl) 4 atoms
Sodium (Na) 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 10-16 (pdb code 5am9). 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 10-16, PDB code: 5am9:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 5am9

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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 10-16


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 10-16 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1001

b:20.9
occ:1.00
 OE1 A:GLU389 2.0 21.0 1.0
O A:HOH2273 2.0 17.3 1.0
NE2 A:HIS365 2.1 20.3 1.0
NE2 A:HIS361 2.1 18.9 1.0
CD A:GLU389 2.9 20.5 1.0
CE1 A:HIS365 2.9 20.8 1.0
CE1 A:HIS361 3.0 19.5 1.0
CD2 A:HIS361 3.1 18.8 1.0
CD2 A:HIS365 3.1 20.8 1.0
OE2 A:GLU389 3.2 19.8 1.0
O A:HOH2254 3.8 25.9 1.0
N A:GLN915 4.0 26.3 1.0
CE1 A:TYR501 4.0 18.7 1.0
ND1 A:HIS365 4.1 20.8 1.0
ND1 A:HIS361 4.1 19.5 1.0
CG A:HIS361 4.2 19.1 1.0
OH A:TYR501 4.2 19.6 1.0
CG A:HIS365 4.2 20.4 1.0
CG A:GLU389 4.3 21.2 1.0
CA A:GLN915 4.3 26.1 1.0
O A:HOH2282 4.4 20.1 1.0
OE2 A:GLU362 4.5 19.8 1.0
CZ A:TYR501 4.6 19.0 1.0
CA A:GLU389 4.6 21.1 1.0
CB A:GLU389 4.7 21.1 1.0
OE1 A:GLU362 4.7 21.4 1.0
C A:GLN915 4.8 25.5 1.0
O A:HOH2253 4.9 30.0 1.0
CD A:GLU362 4.9 20.2 1.0

Zinc binding site 2 out of 4 in 5am9

Go back to Zinc Binding Sites List in 5am9
Zinc binding site 2 out of 4 in the Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 10-16


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 10-16 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1001

b:18.5
occ:1.00
 OE1 B:GLU389 2.0 16.8 1.0
O B:HOH2273 2.1 15.3 1.0
NE2 B:HIS361 2.1 17.6 1.0
NE2 B:HIS365 2.1 18.7 1.0
CD B:GLU389 2.9 16.7 1.0
CE1 B:HIS365 2.9 18.7 1.0
CE1 B:HIS361 3.0 18.2 1.0
CD2 B:HIS361 3.1 17.5 1.0
OE2 B:GLU389 3.1 16.4 1.0
CD2 B:HIS365 3.2 18.9 1.0
O B:HOH2250 3.9 26.6 1.0
N B:GLU911 3.9 22.2 1.0
CE1 B:TYR501 4.0 18.1 1.0
ND1 B:HIS365 4.1 19.1 1.0
ND1 B:HIS361 4.1 17.9 1.0
OH B:TYR501 4.1 18.2 1.0
CG B:HIS361 4.2 17.4 1.0
CG B:GLU389 4.3 17.0 1.0
CG B:HIS365 4.3 18.7 1.0
CA B:GLU911 4.3 23.1 1.0
O B:HOH2284 4.5 20.9 1.0
CZ B:TYR501 4.6 18.1 1.0
OE2 B:GLU362 4.6 19.1 1.0
CA B:GLU389 4.6 17.6 1.0
CB B:GLU389 4.7 17.5 1.0
OE1 B:GLU362 4.7 19.0 1.0
C B:GLU911 4.8 22.6 1.0
CD B:GLU362 4.9 18.9 1.0
O B:HOH2249 5.0 43.5 1.0

Zinc binding site 3 out of 4 in 5am9

Go back to Zinc Binding Sites List in 5am9
Zinc binding site 3 out of 4 in the Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 10-16


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 10-16 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn1001

b:17.9
occ:1.00
 OE1 C:GLU389 1.9 16.9 1.0
O C:HOH2329 2.1 11.4 1.0
NE2 C:HIS361 2.1 16.7 1.0
NE2 C:HIS365 2.1 17.0 1.0
CD C:GLU389 2.9 17.0 1.0
CE1 C:HIS365 2.9 16.8 1.0
CE1 C:HIS361 3.0 16.6 1.0
CD2 C:HIS361 3.1 16.6 1.0
OE2 C:GLU389 3.2 17.6 1.0
CD2 C:HIS365 3.2 16.8 1.0
O C:HOH2305 3.7 30.0 1.0
CE1 C:TYR501 4.0 16.5 1.0
N C:GLU911 4.0 21.6 1.0
OH C:TYR501 4.1 17.0 1.0
ND1 C:HIS365 4.1 17.0 1.0
ND1 C:HIS361 4.1 15.9 1.0
CG C:HIS361 4.2 15.6 1.0
CG C:GLU389 4.2 17.3 1.0
CG C:HIS365 4.3 16.8 1.0
O C:HOH2340 4.4 20.6 1.0
CA C:GLU911 4.4 21.4 1.0
CZ C:TYR501 4.5 17.1 1.0
CA C:GLU389 4.5 17.0 1.0
CB C:GLU389 4.6 17.2 1.0
OE2 C:GLU362 4.7 18.2 1.0
OE1 C:GLU362 4.7 18.1 1.0
C C:GLU911 4.8 20.6 1.0
O C:HOH2304 4.9 32.2 1.0

Zinc binding site 4 out of 4 in 5am9

Go back to Zinc Binding Sites List in 5am9
Zinc binding site 4 out of 4 in the Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 10-16


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 10-16 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn1001

b:19.5
occ:1.00
 OE1 D:GLU389 1.9 20.0 1.0
O D:HOH2277 2.0 15.1 1.0
NE2 D:HIS365 2.0 18.8 1.0
NE2 D:HIS361 2.1 18.1 1.0
CD D:GLU389 2.9 19.2 1.0
CE1 D:HIS365 2.9 18.7 1.0
CE1 D:HIS361 3.1 17.3 1.0
CD2 D:HIS361 3.1 17.5 1.0
CD2 D:HIS365 3.1 18.3 1.0
OE2 D:GLU389 3.2 19.1 1.0
O D:HOH2259 3.7 31.8 1.0
N D:GLN915 4.0 27.4 1.0
CE1 D:TYR501 4.0 17.9 1.0
ND1 D:HIS365 4.1 18.4 1.0
ND1 D:HIS361 4.2 17.3 1.0
OH D:TYR501 4.2 18.7 1.0
CG D:HIS365 4.2 18.0 1.0
CG D:HIS361 4.2 17.0 1.0
CG D:GLU389 4.3 19.2 1.0
CA D:GLN915 4.4 27.1 1.0
O D:HOH2287 4.4 19.7 1.0
CA D:GLU389 4.6 19.7 1.0
CZ D:TYR501 4.6 18.2 1.0
OE1 D:GLU362 4.7 18.6 1.0
OE2 D:GLU362 4.7 19.6 1.0
CB D:GLU389 4.7 19.8 1.0
C D:GLN915 4.8 26.4 1.0
O D:HOH2258 4.8 40.0 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 13:04:59 2024

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