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Calcium 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:

Zinc (Zn) 4 atoms
Chlorine (Cl) 4 atoms
Sodium (Na) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium 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 Calcium atom.
In total 2 binding sites of Calcium 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 Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 5am9

Go back to Calcium Binding Sites List in 5am9
Calcium binding site 1 out of 2 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 Calcium with other atoms in the Ca 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
B:Ca1003

b:41.5
occ:1.00
OE2 B:GLU262 2.1 30.0 1.0
O B:HOH2198 2.3 30.1 1.0
O B:HOH2205 2.5 26.9 1.0
OD2 B:ASP354 2.5 29.8 1.0
OD1 B:ASN263 2.6 27.4 1.0
O B:HOH2207 2.7 32.9 1.0
CD B:GLU262 3.3 27.4 1.0
CG B:ASP354 3.5 27.3 1.0
CG B:ASN263 3.6 26.0 1.0
ND2 B:ASN263 4.0 25.0 1.0
CB B:ASP354 4.0 24.0 1.0
CG B:GLU262 4.1 25.7 1.0
O B:HOH2196 4.2 19.2 1.0
OE1 B:GLU262 4.2 25.6 1.0
O B:HOH2203 4.3 37.7 1.0
O B:HOH2201 4.3 34.6 1.0
OG B:SER260 4.3 20.5 1.0
OD1 B:ASP354 4.3 30.4 1.0
O B:HOH2049 4.6 27.6 1.0
OD1 B:ASP255 4.6 22.2 1.0
O B:HOH2264 4.8 28.3 1.0
CB B:ASN263 4.9 24.8 1.0
O B:HOH2109 5.0 19.8 1.0
O B:GLY254 5.0 22.0 1.0

Calcium binding site 2 out of 2 in 5am9

Go back to Calcium Binding Sites List in 5am9
Calcium binding site 2 out of 2 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 Calcium with other atoms in the Ca 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
C:Ca1003

b:25.6
occ:1.00
OE2 C:GLU262 2.2 22.4 1.0
O C:HOH2250 2.3 19.6 1.0
O C:HOH2244 2.3 19.7 1.0
OD2 C:ASP354 2.4 24.5 1.0
O C:HOH2252 2.5 22.4 1.0
OD1 C:ASN263 2.5 21.9 1.0
CD C:GLU262 3.4 20.8 1.0
CG C:ASP354 3.4 23.1 1.0
CG C:ASN263 3.5 20.6 1.0
ND2 C:ASN263 3.8 20.3 1.0
CB C:ASP354 3.9 21.3 1.0
O C:HOH2316 4.1 26.8 1.0
CG C:GLU262 4.1 20.0 1.0
O C:HOH2243 4.2 15.6 1.0
O C:HOH2248 4.2 20.8 1.0
OE1 C:GLU262 4.2 20.0 1.0
O C:HOH2089 4.4 20.7 1.0
OG C:SER260 4.4 18.5 1.0
OD1 C:ASP354 4.4 24.6 1.0
O C:HOH2059 4.5 24.9 1.0
OD2 C:ASP255 4.7 19.2 1.0
O C:HOH2321 4.8 22.4 1.0
CB C:ASN263 4.8 19.3 1.0
O C:HOH2137 4.8 14.4 1.0
O C:GLY254 5.0 17.8 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 Jul 9 04:13:32 2025

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