Rhenium in PDB 5k1n: Human Ttr Altered By A Rhenium Tris-Carbonyl Pyta-C12 Derivative

The structure of Human Ttr Altered By A Rhenium Tris-Carbonyl Pyta-C12 Derivative, PDB code: 5k1n was solved by E.A.Stura, L.Ciccone, W.Shepard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.07 / 1.81
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	42.650, 82.130, 67.720, 90.00, 90.00, 90.00
R / Rfree (%)	18.9 / 22.4

The binding sites of Rhenium atom in the Human Ttr Altered By A Rhenium Tris-Carbonyl Pyta-C12 Derivative (pdb code 5k1n). This binding sites where shown within 5.0 Angstroms radius around Rhenium atom.
In total 3 binding sites of Rhenium where determined in the Human Ttr Altered By A Rhenium Tris-Carbonyl Pyta-C12 Derivative, PDB code: 5k1n:
Jump to Rhenium binding site number: 1; 2; 3;

Rhenium binding site 1 out of 3 in the Human Ttr Altered By A Rhenium Tris-Carbonyl Pyta-C12 Derivative


Mono view


Stereo pair view

A full contact list of Rhenium with other atoms in the Re binding site number 1 of Human Ttr Altered By A Rhenium Tris-Carbonyl Pyta-C12 Derivative within 5.0Å range: probe atom residue distance (Å) B Occ A:Re204 b:39.3 occ:0.20 O A:HOH322 2.5 36.6 1.0 O B:HOH351 2.6 37.8 0.4 N B:VAL94 2.7 18.1 1.0 O B:HOH351 2.7 29.4 0.6 O A:HIS90 2.8 36.6 1.0 N A:HIS90 3.0 16.9 1.0 N A:GLU89 3.0 24.9 1.0 CA B:VAL93 3.5 18.9 1.0 O B:VAL94 3.5 20.0 1.0 C B:VAL93 3.5 21.9 1.0 C A:HIS90 3.7 23.3 1.0 CA B:VAL94 3.8 16.9 1.0 CB A:HIS88 3.8 21.5 1.0 CA A:GLU89 3.8 20.0 1.0 CA A:HIS90 3.8 17.1 1.0 C A:GLU89 3.9 24.8 1.0 CB A:GLU89 4.0 25.1 1.0 C A:HIS88 4.0 26.5 1.0 CB B:VAL93 4.0 18.9 1.0 C B:VAL94 4.1 14.8 1.0 CA A:HIS88 4.1 18.3 1.0 CB B:VAL94 4.1 17.6 1.0 CB A:HIS90 4.2 25.1 1.0 CD2 A:HIS88 4.5 18.3 1.0 CG A:HIS88 4.5 18.8 1.0 O B:GLU92 4.6 18.8 0.7 CG1 B:VAL93 4.6 19.2 1.0 N B:VAL93 4.7 20.2 1.0 O B:VAL93 4.7 19.9 1.0 CD2 A:HIS90 4.8 30.8 1.0 O B:GLU92 4.8 15.3 0.3 OE2 B:GLU92 4.8 57.0 0.7 CG A:HIS90 4.8 27.8 1.0 CG2 B:VAL94 4.9 19.0 1.0 N A:ALA91 5.0 18.9 1.0

Rhenium binding site 2 out of 3 in the Human Ttr Altered By A Rhenium Tris-Carbonyl Pyta-C12 Derivative


Mono view


Stereo pair view

A full contact list of Rhenium with other atoms in the Re binding site number 2 of Human Ttr Altered By A Rhenium Tris-Carbonyl Pyta-C12 Derivative within 5.0Å range: probe atom residue distance (Å) B Occ B:Re202 b:55.5 occ:0.30 NE2 B:HIS88 3.4 56.1 1.0 N A:THR96 3.6 28.2 1.0 CE2 B:TYR114 4.0 29.5 1.0 CA A:PHE95 4.0 27.2 1.0 CD2 B:HIS88 4.1 45.4 1.0 CB A:PHE95 4.1 26.6 1.0 CD2 B:PHE87 4.2 58.8 1.0 O A:THR96 4.3 31.2 1.0 CD2 B:TYR114 4.3 24.9 1.0 C A:PHE95 4.4 26.6 1.0 CB A:THR96 4.4 33.5 1.0 O B:PRO113 4.5 23.2 1.0 CA A:THR96 4.5 28.2 1.0 CE1 B:HIS88 4.5 52.8 1.0 CB B:PHE87 4.6 35.1 1.0 CZ B:TYR114 4.6 32.1 1.0 OG1 A:THR96 4.8 39.6 1.0 CG B:PHE87 4.8 48.1 1.0 C A:THR96 4.9 30.3 1.0

Rhenium binding site 3 out of 3 in the Human Ttr Altered By A Rhenium Tris-Carbonyl Pyta-C12 Derivative


Mono view


Stereo pair view

A full contact list of Rhenium with other atoms in the Re binding site number 3 of Human Ttr Altered By A Rhenium Tris-Carbonyl Pyta-C12 Derivative within 5.0Å range: probe atom residue distance (Å) B Occ B:Re203 b:51.7 occ:0.30 OH B:TYR116 3.1 49.2 1.0 CG2 B:ILE107 4.1 22.9 1.0 OG1 B:THR118 4.2 26.0 1.0 CB B:ALA109 4.2 19.6 1.0 CG1 B:VAL93 4.2 19.2 1.0 CG2 B:ILE73 4.4 18.9 1.0 CZ B:TYR116 4.4 32.6 1.0 CG2 B:VAL93 4.5 15.0 1.0 O B:VAL71 4.6 19.7 1.0 CD1 B:ILE73 4.6 25.4 1.0 CG1 B:VAL71 4.7 18.8 1.0 CG1 B:ILE73 4.8 24.4 1.0 CB B:THR118 4.9 24.8 1.0 N B:VAL93 4.9 20.2 1.0 CB B:VAL93 5.0 18.9 1.0 C B:GLU92 5.0 19.1 0.3

L.Ciccone, C.Policar, E.A.Stura, W.Shepard. Human Ttr Conformation Altered By Rhenium Tris-Carbonyl Derivatives. J.Struct.Biol. V. 195 353 2016.
ISSN: ESSN 1095-8657
PubMed: 27402536
DOI: 10.1016/J.JSB.2016.07.002