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Iodine in PDB 1nuo: Two Rth Mutants with Impaired Hormone Binding

Protein crystallography data

The structure of Two Rth Mutants with Impaired Hormone Binding, PDB code: 1nuo 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) 20.00 / 3.10
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 67.274, 67.274, 130.121, 90.00, 90.00, 120.00
R / Rfree (%) 25.2 / 30.2

Iodine Binding Sites:

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

Iodine binding site 1 out of 3 in 1nuo

Go back to Iodine Binding Sites List in 1nuo
Iodine binding site 1 out of 3 in the Two Rth Mutants with Impaired Hormone Binding


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 1 of Two Rth Mutants with Impaired Hormone Binding within 5.0Å range:
probe atom residue distance (Å) B Occ
A:I500

b:77.9
occ:1.00
I1 A:4HY500 0.0 77.9 1.0
C5 A:4HY500 2.1 80.8 1.0
CD1 A:ILE276 2.6 59.3 1.0
CG1 A:ILE276 2.7 66.5 1.0
C3 A:4HY500 3.0 82.9 1.0
C7 A:4HY500 3.1 82.5 1.0
O2 A:4HY500 3.4 80.1 1.0
O A:PHE272 3.7 86.0 1.0
C2 A:4HY500 3.8 76.5 1.0
CG1 A:ILE275 3.9 81.0 1.0
O A:ILE275 4.0 74.7 1.0
CB A:ILE276 4.0 71.5 1.0
C4 A:4HY500 4.1 78.5 1.0
C A:PHE272 4.2 84.4 1.0
CA A:PHE272 4.2 83.3 1.0
CA A:ILE276 4.2 70.5 1.0
C1 A:4HY500 4.4 84.7 1.0
CB A:PHE272 4.4 82.9 1.0
C9 A:4HY500 4.4 84.0 1.0
C A:ILE275 4.4 75.5 1.0
CD1 A:LEU330 4.5 84.0 1.0
CB A:LEU330 4.5 77.6 1.0
N A:ILE276 4.6 71.9 1.0
CD1 A:ILE275 4.6 82.3 1.0
C12 A:4HY500 4.7 78.7 1.0
C11 A:4HY500 4.8 87.4 1.0

Iodine binding site 2 out of 3 in 1nuo

Go back to Iodine Binding Sites List in 1nuo
Iodine binding site 2 out of 3 in the Two Rth Mutants with Impaired Hormone Binding


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 2 of Two Rth Mutants with Impaired Hormone Binding within 5.0Å range:
probe atom residue distance (Å) B Occ
A:I500

b:81.5
occ:1.00
I2 A:4HY500 0.0 81.5 1.0
C6 A:4HY500 2.1 81.8 1.0
C4 A:4HY500 3.0 78.5 1.0
C8 A:4HY500 3.1 78.8 1.0
O1 A:4HY500 3.3 68.7 1.0
CE1 A:PHE269 3.8 66.3 1.0
CD1 A:PHE269 3.8 66.1 1.0
SD A:MET442 4.1 84.8 1.0
CD2 A:LEU346 4.1 76.6 1.0
C10 A:4HY500 4.3 82.5 1.0
C2 A:4HY500 4.3 76.5 1.0
CB A:PHE272 4.4 82.9 1.0
CG A:LEU346 4.5 71.3 1.0
CD1 A:PHE272 4.5 78.0 1.0
O A:GLY344 4.5 59.0 1.0
CE A:MET442 4.6 86.4 1.0
C12 A:4HY500 4.8 78.7 1.0
O A:GLY345 4.9 69.8 1.0
CZ A:PHE269 4.9 61.8 1.0
CG A:PHE272 4.9 78.0 1.0
CG A:PHE269 5.0 68.5 1.0

Iodine binding site 3 out of 3 in 1nuo

Go back to Iodine Binding Sites List in 1nuo
Iodine binding site 3 out of 3 in the Two Rth Mutants with Impaired Hormone Binding


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 3 of Two Rth Mutants with Impaired Hormone Binding within 5.0Å range:
probe atom residue distance (Å) B Occ
A:I500

b:79.7
occ:1.00
I3 A:4HY500 0.0 79.7 1.0
C9 A:4HY500 2.0 84.0 1.0
C7 A:4HY500 3.0 82.5 1.0
C11 A:4HY500 3.0 87.4 1.0
O2 A:4HY500 3.0 80.1 1.0
CD1 A:ILE353 3.4 48.4 1.0
C2 A:4HY500 3.6 76.5 1.0
C12 A:4HY500 3.7 78.7 1.0
CB A:ALA317 4.0 62.2 1.0
CE A:MET310 4.0 54.2 1.0
CD2 A:LEU341 4.1 62.1 1.0
C5 A:4HY500 4.3 80.8 1.0
C1 A:4HY500 4.3 84.7 1.0
CD1 A:LEU346 4.4 70.2 1.0
CD2 A:LEU330 4.6 76.5 1.0
CG2 A:ILE353 4.8 58.2 1.0
C3 A:4HY500 4.8 82.9 1.0
CG1 A:ILE353 4.8 57.2 1.0
CD1 A:LEU341 4.8 52.7 1.0
C4 A:4HY500 4.8 78.5 1.0
C10 A:4HY500 4.9 82.5 1.0
O A:MET313 4.9 56.6 1.0

Reference:

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
Page generated: Sun Aug 11 12:31:34 2024

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