Arsenic in PDB 1nq2: Two Rth Mutants with Impaired Hormone Binding

The structure of Two Rth Mutants with Impaired Hormone Binding, PDB code: 1nq2 was solved by B.R.Huber, B.Sandler, B.L.West, S.T.Cunha-Lima, H.T.Nguyen, J.W.Apriletti, J.D.Baxter, R.J.Fletterick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.40
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	68.954, 68.954, 131.400, 90.00, 90.00, 120.00
R / Rfree (%)	22.7 / 26.4

The structure of Two Rth Mutants with Impaired Hormone Binding also contains other interesting chemical elements:

Iodine	(I)	3 atoms
Sodium	(Na)	1 atom

The binding sites of Arsenic atom in the Two Rth Mutants with Impaired Hormone Binding (pdb code 1nq2). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 5 binding sites of Arsenic where determined in the Two Rth Mutants with Impaired Hormone Binding, PDB code: 1nq2:
Jump to Arsenic binding site number: 1; 2; 3; 4; 5;

Arsenic binding site 1 out of 5 in the Two Rth Mutants with Impaired Hormone Binding


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Two Rth Mutants with Impaired Hormone Binding within 5.0Å range: probe atom residue distance (Å) B Occ A:As600 b:81.9 occ:0.59 SG A:CYS298 2.9 62.8 1.0 CB A:CYS298 3.6 54.7 1.0 N A:GLU299 3.7 54.6 1.0 CA A:GLU299 4.0 55.6 1.0 C A:CYS298 4.0 54.3 1.0 OE1 A:GLU299 4.0 70.1 1.0 CG A:GLU299 4.2 64.7 1.0 CD A:GLU299 4.2 67.8 1.0 O A:CYS298 4.3 54.0 1.0 CD1 A:ILE302 4.4 49.5 1.0 CG1 A:ILE302 4.4 48.6 1.0 CA A:CYS298 4.5 54.8 1.0 CB A:GLU299 4.7 59.3 1.0 OE2 A:GLU299 5.0 68.6 1.0

Arsenic binding site 2 out of 5 in the Two Rth Mutants with Impaired Hormone Binding


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of Two Rth Mutants with Impaired Hormone Binding within 5.0Å range: probe atom residue distance (Å) B Occ A:As601 b:59.8 occ:0.59 SG A:CYS294 2.7 50.3 1.0 CB A:CYS294 3.4 48.3 1.0 CA A:CYS294 4.0 49.1 1.0 O A:LYS288 4.7 38.3 1.0 N A:CYS294 4.9 46.1 1.0 NE2 A:GLN301 5.0 41.0 1.0 CG A:LYS288 5.0 37.6 1.0 O A:CYS294 5.0 51.1 1.0

Arsenic binding site 3 out of 5 in the Two Rth Mutants with Impaired Hormone Binding


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 3 of Two Rth Mutants with Impaired Hormone Binding within 5.0Å range: probe atom residue distance (Å) B Occ A:As602 b:81.4 occ:0.79 O A:HOH952 2.8 66.3 1.0 SG A:CYS388 2.9 56.2 1.0 CB A:CYS388 3.3 55.6 1.0 O A:HOH930 3.5 91.1 1.0 O A:HOH913 3.6 46.4 1.0 NH2 A:ARG391 3.7 73.6 1.0 NE A:ARG391 3.7 70.8 1.0 CZ A:ARG391 4.1 72.9 1.0 CA A:CYS388 4.2 54.9 1.0 CB A:ARG391 4.3 57.8 1.0 CD A:ARG391 4.8 67.7 1.0 CG A:ARG391 4.9 62.7 1.0 O A:HOH931 4.9 79.2 1.0

Arsenic binding site 4 out of 5 in the Two Rth Mutants with Impaired Hormone Binding


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 4 of Two Rth Mutants with Impaired Hormone Binding within 5.0Å range: probe atom residue distance (Å) B Occ A:As603 b:76.0 occ:1.00 SG A:CYS434 2.8 48.3 1.0 O A:CYS434 3.8 33.7 1.0 CB A:CYS434 3.9 37.3 1.0 CA A:CYS434 4.0 33.9 1.0 CB A:SER437 4.0 37.5 1.0 OG A:SER437 4.1 37.6 1.0 AS A:ARS604 4.3 77.5 0.6 C A:CYS434 4.4 34.0 1.0

Arsenic binding site 5 out of 5 in the Two Rth Mutants with Impaired Hormone Binding


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 5 of Two Rth Mutants with Impaired Hormone Binding within 5.0Å range: probe atom residue distance (Å) B Occ A:As604 b:77.5 occ:0.59 SG A:CYS434 3.0 48.3 1.0 CB A:CYS434 3.7 37.3 1.0 AS A:ARS603 4.3 76.0 1.0 CG1 A:VAL348 4.8 28.7 1.0 CB A:VAL348 5.0 30.8 1.0

B.R.Huber, B.Sandler, B.L.West, S.T.Cunha-Lima, H.T.Nguyen, J.W.Apriletti, J.D.Baxter, R.J.Fletterick. Two Resistance to Thyroid Hormone Mutants with Impaired Hormone Binding Mol.Endocrinol. V. 17 643 2003.
ISSN: ISSN 0888-8809
PubMed: 12554782
DOI: 10.1210/ME.2002-0095