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Copper in PDB 5n7c: Human Ttr Altered Conformation From Soaking in CUCL2.

Protein crystallography data

The structure of Human Ttr Altered Conformation From Soaking in CUCL2., PDB code: 5n7c was solved by L.Ciccone, M.Savko, W.Shepard, E.A.Stura, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.27 / 2.45
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 42.990, 82.540, 67.770, 90.00, 90.00, 90.00
R / Rfree (%) 16.9 / 25.4

Copper Binding Sites:

The binding sites of Copper atom in the Human Ttr Altered Conformation From Soaking in CUCL2. (pdb code 5n7c). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Human Ttr Altered Conformation From Soaking in CUCL2., PDB code: 5n7c:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 5n7c

Go back to Copper Binding Sites List in 5n7c
Copper binding site 1 out of 4 in the Human Ttr Altered Conformation From Soaking in CUCL2.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Human Ttr Altered Conformation From Soaking in CUCL2. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu201

b:79.2
occ:0.50
OD1 A:ASP74 2.5 57.7 1.0
O A:HOH301 2.6 58.0 1.0
NE2 A:HIS90 2.8 63.5 1.0
O A:HOH368 3.0 50.3 1.0
CG A:ASP74 3.3 51.7 1.0
CD2 A:HIS90 3.4 57.2 1.0
OD2 A:ASP74 3.7 65.7 1.0
CE1 A:HIS90 3.9 69.8 1.0
OE1 A:GLU72 4.1 61.1 1.0
CB A:ASP74 4.5 46.8 1.0
CG A:HIS90 4.6 55.4 1.0
ND1 A:HIS90 4.8 56.6 1.0
CD A:GLU72 4.9 59.0 1.0
CG A:GLU72 4.9 46.6 1.0
ND1 A:HIS31 4.9 33.1 1.0
OE2 A:GLU89 5.0 52.5 0.5

Copper binding site 2 out of 4 in 5n7c

Go back to Copper Binding Sites List in 5n7c
Copper binding site 2 out of 4 in the Human Ttr Altered Conformation From Soaking in CUCL2.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Human Ttr Altered Conformation From Soaking in CUCL2. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu201

b:93.5
occ:0.50
O A:HOH306 2.4 63.8 1.0
OE2 A:GLU89 2.7 52.5 0.5
OE1 A:GLU89 2.8 59.6 0.5
O A:HOH337 2.8 57.7 1.0
CD A:GLU89 2.8 55.1 0.5
O A:HOH348 3.8 39.9 1.0
CG A:GLU89 3.9 51.5 0.5
CG A:GLU89 4.0 46.8 0.5
CD A:LYS76 4.1 52.8 1.0
OE2 A:GLU89 4.2 49.9 0.5
O A:HOH329 4.5 55.0 1.0
CD A:GLU89 4.6 46.5 0.5
CB A:LYS76 4.6 40.8 1.0
CG A:LYS76 4.7 47.2 1.0
CB A:GLU89 5.0 46.8 0.5
NE2 A:HIS90 5.0 63.5 1.0

Copper binding site 3 out of 4 in 5n7c

Go back to Copper Binding Sites List in 5n7c
Copper binding site 3 out of 4 in the Human Ttr Altered Conformation From Soaking in CUCL2.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Human Ttr Altered Conformation From Soaking in CUCL2. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu201

b:0.6
occ:1.00
NE2 B:HIS90 2.2 88.5 1.0
CE1 B:HIS90 2.6 79.9 1.0
NE2 B:HIS88 2.8 0.7 1.0
O B:HOH381 3.1 43.9 1.0
CE1 B:HIS88 3.1 0.1 1.0
O B:HOH365 3.1 75.9 1.0
O B:HOH372 3.3 51.4 1.0
CD2 B:HIS90 3.4 83.1 1.0
NZ B:LYS76 3.7 64.6 1.0
ND1 B:HIS90 3.9 79.9 1.0
OD2 B:ASP74 4.0 70.2 1.0
CD2 B:HIS88 4.0 0.8 1.0
OD1 B:ASP74 4.2 58.6 1.0
CG B:HIS90 4.3 75.1 1.0
ND1 B:HIS88 4.4 0.2 1.0
CG B:ASP74 4.5 60.6 1.0
CE B:LYS76 4.7 68.6 1.0
CD B:LYS76 4.8 68.2 1.0
CG B:HIS88 4.9 0.5 1.0

Copper binding site 4 out of 4 in 5n7c

Go back to Copper Binding Sites List in 5n7c
Copper binding site 4 out of 4 in the Human Ttr Altered Conformation From Soaking in CUCL2.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Human Ttr Altered Conformation From Soaking in CUCL2. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu202

b:0.4
occ:1.00
O B:HOH386 3.3 61.8 1.0
CB B:ALA37 3.8 76.0 1.0
O B:HOH376 3.9 62.5 1.0
N B:ASP38 4.1 69.6 1.0
N B:ALA37 4.1 65.4 1.0
CG B:ASP38 4.2 85.5 1.0
OD2 B:ASP38 4.2 86.7 1.0
CB B:ALA36 4.3 51.9 1.0
CA B:ALA37 4.4 73.1 1.0
CB B:ASP38 4.5 80.4 1.0
OD1 B:ASP38 4.5 90.7 1.0
C B:ALA37 4.7 70.7 1.0
C B:ALA36 4.9 55.6 1.0
CA B:ASP38 5.0 76.2 1.0

Reference:

L.Ciccone, C.Fruchart-Gaillard, G.Mourier, M.Savko, S.Nencetti, E.Orlandini, D.Servent, E.A.Stura, W.Shepard. Copper Mediated Amyloid-Beta Binding to Transthyretin. Sci Rep V. 8 13744 2018.
ISSN: ESSN 2045-2322
PubMed: 30213975
DOI: 10.1038/S41598-018-31808-5
Page generated: Wed Jul 31 04:42:48 2024

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