Zinc in PDB 5amb: Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 35-42

Enzymatic activity of Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 35-42

All present enzymatic activity of Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 35-42:
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 35-42, PDB code: 5amb 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) 74.51 / 1.55
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 72.979, 76.950, 83.219, 88.63, 64.14, 75.22
R / Rfree (%) 15.75 / 18.115

Other elements in 5amb:

The structure of Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 35-42 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 35-42 (pdb code 5amb). 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 35-42, PDB code: 5amb:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 5amb

Go back to Zinc Binding Sites List in 5amb
Zinc binding site 1 out of 2 in the Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 35-42


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 35-42 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1001

b:25.1
occ:1.00
O A:HOH2346 2.0 29.8 1.0
OE1 A:GLU389 2.0 23.2 1.0
NE2 A:HIS361 2.0 23.5 1.0
NE2 A:HIS365 2.0 22.8 1.0
O A:HOH2347 2.5 41.9 1.0
CE1 A:HIS361 3.0 24.4 1.0
CD A:GLU389 3.0 23.4 1.0
CE1 A:HIS365 3.0 19.6 1.0
CD2 A:HIS361 3.0 24.2 1.0
CD2 A:HIS365 3.1 22.9 1.0
OE2 A:GLU389 3.3 24.9 1.0
N P:ILE41 3.7 30.2 1.0
ND1 A:HIS361 4.1 23.1 1.0
ND1 A:HIS365 4.1 23.9 1.0
CE1 A:TYR501 4.1 23.8 1.0
OH A:TYR501 4.1 25.0 1.0
CG A:HIS361 4.1 23.7 1.0
CA P:ILE41 4.2 31.5 1.0
CG A:HIS365 4.2 21.4 1.0
O A:HOH2324 4.3 51.1 1.0
CG A:GLU389 4.3 21.4 1.0
O A:HOH2358 4.4 28.4 1.0
OE1 A:GLU362 4.5 28.1 1.0
OE2 A:GLU362 4.6 28.9 1.0
O A:HOH2323 4.6 42.8 1.0
CA A:GLU389 4.6 24.4 1.0
CZ A:TYR501 4.6 25.5 1.0
C P:ILE41 4.7 29.0 1.0
CB A:GLU389 4.7 22.6 1.0
CD A:GLU362 4.9 29.1 1.0
O7 A:P6G1205 5.0 55.1 1.0

Zinc binding site 2 out of 2 in 5amb

Go back to Zinc Binding Sites List in 5amb
Zinc binding site 2 out of 2 in the Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Amyloid-Beta 35-42


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 35-42 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1001

b:25.9
occ:1.00
O B:HOH2264 1.9 27.1 1.0
OE1 B:GLU389 2.0 27.3 1.0
NE2 B:HIS361 2.0 22.5 1.0
NE2 B:HIS365 2.1 26.6 1.0
O B:HOH2265 2.2 47.6 1.0
CE1 B:HIS361 2.9 21.5 1.0
CD B:GLU389 3.0 26.9 1.0
CE1 B:HIS365 3.0 25.1 1.0
CD2 B:HIS361 3.1 22.7 1.0
CD2 B:HIS365 3.1 26.6 1.0
OE2 B:GLU389 3.2 32.2 1.0
N Q:ILE41 3.8 31.4 1.0
O B:HOH2241 4.0 47.6 1.0
ND1 B:HIS361 4.0 25.1 1.0
ND1 B:HIS365 4.1 28.4 1.0
CE1 B:TYR501 4.1 26.0 1.0
CG B:HIS361 4.2 21.4 1.0
OH B:TYR501 4.2 25.4 1.0
CG B:HIS365 4.2 24.3 1.0
CA Q:ILE41 4.3 29.7 1.0
O B:HOH2271 4.3 28.5 1.0
CG B:GLU389 4.3 23.6 1.0
OE1 B:GLU362 4.5 27.6 1.0
OE2 B:GLU362 4.6 29.1 1.0
CA B:GLU389 4.6 25.7 1.0
CZ B:TYR501 4.6 25.2 1.0
O B:HOH2240 4.7 45.5 1.0
CB B:GLU389 4.8 25.3 1.0
C Q:ILE41 4.8 26.0 1.0
CD B:GLU362 4.8 29.5 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: Wed Dec 16 06:03:46 2020

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