Iron in PDB 5n5q: Human Ttr Altered Conformation From Soaking in Iron Chloride.

The structure of Human Ttr Altered Conformation From Soaking in Iron Chloride., PDB code: 5n5q 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)	40.90 / 2.53
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	42.730, 81.810, 69.460, 90.00, 90.00, 90.00
R / Rfree (%)	19.2 / 25.3

The binding sites of Iron atom in the Human Ttr Altered Conformation From Soaking in Iron Chloride. (pdb code 5n5q). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 8 binding sites of Iron where determined in the Human Ttr Altered Conformation From Soaking in Iron Chloride., PDB code: 5n5q:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Iron binding site 1 out of 8 in the Human Ttr Altered Conformation From Soaking in Iron Chloride.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Human Ttr Altered Conformation From Soaking in Iron Chloride. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe202 b:0.6 occ:1.00 FE1 A:FFE202 0.0 0.6 1.0 O05 A:FFE202 2.1 0.6 1.0 O01 A:FFE202 2.1 0.7 1.0 O06 A:FFE202 2.1 0.1 1.0 O03 A:FFE202 2.1 0.8 1.0 O07 A:FFE202 2.1 0.4 1.0 OE2 A:GLU51 2.5 94.5 1.0 OE1 A:GLU51 2.8 88.0 1.0 CD A:GLU51 3.0 82.3 1.0 FE2 A:FFE202 3.5 0.9 1.0 O A:HOH321 3.6 53.1 1.0 O09 A:FFE202 3.7 0.7 1.0 CG A:GLU51 4.4 69.2 1.0

Iron binding site 2 out of 8 in the Human Ttr Altered Conformation From Soaking in Iron Chloride.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Human Ttr Altered Conformation From Soaking in Iron Chloride. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe202 b:0.9 occ:1.00 FE2 A:FFE202 0.0 0.9 1.0 O09 A:FFE202 2.1 0.7 1.0 O10 A:FFE202 2.1 0.9 1.0 O11 A:FFE202 2.1 0.4 1.0 O07 A:FFE202 2.1 0.4 1.0 OE1 A:GLU51 2.6 88.0 1.0 O05 A:FFE202 3.2 0.6 1.0 O14 A:FFE202 3.4 0.4 1.0 O16 A:FFE202 3.4 0.0 1.0 FE3 A:FFE202 3.5 0.9 1.0 FE1 A:FFE202 3.5 0.6 1.0 CD A:GLU51 3.7 82.3 1.0 O A:HOH317 3.9 49.3 1.0 OE2 A:GLU51 4.3 94.5 1.0 O15 A:FFE202 4.3 0.8 1.0 O03 A:FFE202 4.4 0.8 1.0 O01 A:FFE202 4.8 0.7 1.0 CG A:GLU51 4.9 69.2 1.0 O13 A:FFE202 4.9 0.8 1.0

Iron binding site 3 out of 8 in the Human Ttr Altered Conformation From Soaking in Iron Chloride.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Human Ttr Altered Conformation From Soaking in Iron Chloride. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe202 b:0.9 occ:1.00 FE3 A:FFE202 0.0 0.9 1.0 O13 A:FFE202 2.1 0.8 1.0 O15 A:FFE202 2.1 0.8 1.0 O17 A:FFE202 2.1 0.3 1.0 O16 A:FFE202 2.1 0.0 1.0 O14 A:FFE202 2.1 0.4 1.0 O11 A:FFE202 2.1 0.4 1.0 FE2 A:FFE202 3.5 0.9 1.0 O A:HOH302 3.8 78.5 1.0 O10 A:FFE202 3.8 0.9 1.0 O A:HOH303 4.1 55.9 1.0 O09 A:FFE202 4.3 0.7 1.0 O A:HOH317 4.6 49.3 1.0 OE1 A:GLU51 4.9 88.0 1.0

Iron binding site 4 out of 8 in the Human Ttr Altered Conformation From Soaking in Iron Chloride.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Human Ttr Altered Conformation From Soaking in Iron Chloride. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe203 b:98.3 occ:1.00 O A:HOH318 2.1 70.6 1.0 OE2 A:GLU54 2.9 87.5 1.0 CD A:GLU54 3.8 78.6 1.0 OE1 A:GLU54 4.2 88.7 1.0 SD A:MET13 4.5 0.7 1.0 O A:HOH327 4.5 60.3 1.0 CE A:MET13 4.5 0.8 1.0

Iron binding site 5 out of 8 in the Human Ttr Altered Conformation From Soaking in Iron Chloride.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Human Ttr Altered Conformation From Soaking in Iron Chloride. within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe203 b:75.5 occ:1.00 NE2 B:HIS88 2.0 94.6 1.0 CE1 B:HIS88 2.8 87.2 1.0 CD2 B:HIS88 3.1 87.8 1.0 O A:HOH338 3.5 81.4 1.0 N A:THR96 3.7 47.3 1.0 CA A:PHE95 3.8 42.3 1.0 CB A:PHE95 3.9 44.0 1.0 ND1 B:HIS88 4.0 72.9 1.0 CG B:HIS88 4.2 78.0 1.0 CE2 B:TYR114 4.3 45.4 1.0 C A:PHE95 4.3 42.4 1.0 O B:PRO113 4.4 46.5 1.0 CD2 B:TYR114 4.5 44.2 1.0 CB B:PHE87 4.5 93.2 1.0 O A:THR96 4.6 46.0 1.0 O A:VAL94 4.6 43.4 1.0 CB A:THR96 4.6 49.5 1.0 CA A:THR96 4.7 50.3 1.0 OG1 A:THR96 5.0 50.2 1.0 CG B:PHE87 5.0 0.8 1.0

Iron binding site 6 out of 8 in the Human Ttr Altered Conformation From Soaking in Iron Chloride.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Human Ttr Altered Conformation From Soaking in Iron Chloride. within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe204 b:0.8 occ:1.00 O B:HOH350 2.0 89.3 1.0 OE2 B:GLU51 2.1 0.0 1.0 CD B:GLU51 3.3 88.8 1.0 FE B:FE206 4.0 0.4 1.0 CB B:GLU51 4.1 64.9 1.0 OE1 B:GLU51 4.2 0.9 1.0 CG B:GLU51 4.2 71.5 1.0

Iron binding site 7 out of 8 in the Human Ttr Altered Conformation From Soaking in Iron Chloride.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Human Ttr Altered Conformation From Soaking in Iron Chloride. within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe205 b:1.0 occ:1.00 O B:HOH322 2.0 0.5 1.0 O B:HOH346 2.0 88.9 1.0 OE2 B:GLU54 2.1 0.4 1.0 O B:HOH352 2.5 58.2 1.0 O B:HOH317 3.0 79.7 1.0 CD B:GLU54 3.1 77.9 1.0 OE1 B:GLU54 3.4 78.8 1.0 CG B:GLU54 4.5 67.8 1.0 NZ B:LYS15 4.6 84.8 1.0 O B:HOH341 4.8 61.1 1.0

Iron binding site 8 out of 8 in the Human Ttr Altered Conformation From Soaking in Iron Chloride.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Human Ttr Altered Conformation From Soaking in Iron Chloride. within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe206 b:0.4 occ:1.00 O B:HOH301 2.0 0.8 1.0 OE1 B:GLU51 2.1 0.9 1.0 CD B:GLU51 2.8 88.8 1.0 OE2 B:GLU51 2.8 0.0 1.0 FE B:FE204 4.0 0.8 1.0 CG B:GLU51 4.3 71.5 1.0

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