Iodine in PDB 2hra: Crystal Structures of the Interacting Domains From Yeast Glutamyl-Trna Synthetase and Trna Aminoacylation and Nuclear Export Cofactor ARC1P Reveal A Novel Function For An Old Fold

All present enzymatic activity of Crystal Structures of the Interacting Domains From Yeast Glutamyl-Trna Synthetase and Trna Aminoacylation and Nuclear Export Cofactor ARC1P Reveal A Novel Function For An Old Fold:
6.1.1.17;

The structure of Crystal Structures of the Interacting Domains From Yeast Glutamyl-Trna Synthetase and Trna Aminoacylation and Nuclear Export Cofactor ARC1P Reveal A Novel Function For An Old Fold, PDB code: 2hra was solved by H.Simader, M.Hothorn, D.Suck, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	80.00 / 1.90
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	51.959, 107.113, 167.865, 90.00, 90.00, 90.00
R / Rfree (%)	21.4 / 26.2

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 30; Page 4, Binding sites: 31 - 40; Page 5, Binding sites: 41 - 44;

Binding sites:

The binding sites of Iodine atom in the Crystal Structures of the Interacting Domains From Yeast Glutamyl-Trna Synthetase and Trna Aminoacylation and Nuclear Export Cofactor ARC1P Reveal A Novel Function For An Old Fold (pdb code 2hra). This binding sites where shown within 5.0 Angstroms radius around Iodine atom.
In total 44 binding sites of Iodine where determined in the Crystal Structures of the Interacting Domains From Yeast Glutamyl-Trna Synthetase and Trna Aminoacylation and Nuclear Export Cofactor ARC1P Reveal A Novel Function For An Old Fold, PDB code: 2hra:
Jump to Iodine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iodine binding site 1 out of 44 in the Crystal Structures of the Interacting Domains From Yeast Glutamyl-Trna Synthetase and Trna Aminoacylation and Nuclear Export Cofactor ARC1P Reveal A Novel Function For An Old Fold


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 1 of Crystal Structures of the Interacting Domains From Yeast Glutamyl-Trna Synthetase and Trna Aminoacylation and Nuclear Export Cofactor ARC1P Reveal A Novel Function For An Old Fold within 5.0Å range: probe atom residue distance (Å) B Occ A:I401 b:42.2 occ:0.70 O A:HOH497 3.6 37.8 1.0 CD A:PRO62 4.1 28.2 1.0 NZ A:LYS65 4.3 38.5 1.0 CD A:LYS65 4.3 32.7 1.0 CB A:ALA61 4.3 29.8 1.0 CG2 A:THR24 4.4 29.8 1.0 CE A:LYS65 4.4 35.6 1.0 CG2 A:VAL56 4.5 29.2 1.0 CG A:PRO62 4.5 28.4 1.0 CG1 A:VAL56 4.5 30.2 1.0 N A:PRO62 4.8 28.2 1.0 CB A:PRO62 4.9 27.0 1.0 CB A:THR24 4.9 28.8 1.0 O A:PRO62 4.9 25.6 1.0 CB A:LYS65 4.9 28.3 1.0

Iodine binding site 2 out of 44 in the Crystal Structures of the Interacting Domains From Yeast Glutamyl-Trna Synthetase and Trna Aminoacylation and Nuclear Export Cofactor ARC1P Reveal A Novel Function For An Old Fold


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 2 of Crystal Structures of the Interacting Domains From Yeast Glutamyl-Trna Synthetase and Trna Aminoacylation and Nuclear Export Cofactor ARC1P Reveal A Novel Function For An Old Fold within 5.0Å range: probe atom residue distance (Å) B Occ A:I402 b:43.3 occ:0.55 CE2 A:PHE109 3.4 32.3 1.0 CD2 A:PHE109 3.7 31.8 1.0 CE A:LYS159 4.2 27.7 1.0 NZ A:LYS159 4.2 31.3 1.0 CA A:ALA110 4.2 26.6 1.0 OG A:SER113 4.4 26.9 1.0 CG B:PRO62 4.5 31.2 1.0 CB A:ALA110 4.5 26.6 1.0 CB A:SER113 4.6 26.3 1.0 CZ A:PHE109 4.6 32.2 1.0 OG1 B:THR70 4.7 25.1 1.0 N A:ALA110 4.8 25.2 1.0 CB B:THR70 4.9 27.8 1.0 CG2 B:THR70 4.9 25.4 1.0 CD B:PRO62 4.9 31.3 1.0

Iodine binding site 3 out of 44 in the Crystal Structures of the Interacting Domains From Yeast Glutamyl-Trna Synthetase and Trna Aminoacylation and Nuclear Export Cofactor ARC1P Reveal A Novel Function For An Old Fold


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 3 of Crystal Structures of the Interacting Domains From Yeast Glutamyl-Trna Synthetase and Trna Aminoacylation and Nuclear Export Cofactor ARC1P Reveal A Novel Function For An Old Fold within 5.0Å range: probe atom residue distance (Å) B Occ A:I403 b:39.2 occ:0.60 N A:LEU133 3.8 31.9 1.0 CB A:LYS134 3.8 29.8 1.0 N A:LYS134 3.9 30.5 1.0 CA A:GLY132 3.9 31.3 1.0 ND2 A:ASN87 3.9 34.7 1.0 O A:HOH523 4.1 40.4 1.0 CB A:ASN87 4.3 38.7 1.0 C A:GLY132 4.3 31.3 1.0 CA A:LYS134 4.5 29.9 1.0 O A:LYS134 4.5 28.3 1.0 CD A:LYS134 4.5 33.3 1.0 CG A:ASN87 4.6 37.8 1.0 CE A:LYS134 4.6 34.2 1.0 CA A:LEU133 4.7 32.4 1.0 CG A:LYS134 4.7 32.9 1.0 C A:LEU133 4.8 31.9 1.0 CB A:LEU133 4.9 33.3 1.0 C A:LYS134 5.0 28.5 1.0

Iodine binding site 4 out of 44 in the Crystal Structures of the Interacting Domains From Yeast Glutamyl-Trna Synthetase and Trna Aminoacylation and Nuclear Export Cofactor ARC1P Reveal A Novel Function For An Old Fold


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 4 of Crystal Structures of the Interacting Domains From Yeast Glutamyl-Trna Synthetase and Trna Aminoacylation and Nuclear Export Cofactor ARC1P Reveal A Novel Function For An Old Fold within 5.0Å range: probe atom residue distance (Å) B Occ A:I406 b:36.7 occ:0.45 O A:ASN87 2.7 40.6 1.0 OD1 A:ASN87 3.3 37.5 1.0 C A:PHE85 3.5 34.3 1.0 N A:ALA137 3.6 25.6 1.0 N A:ASN87 3.7 38.2 1.0 O A:PHE85 3.7 34.7 1.0 CA A:PHE85 3.7 33.4 1.0 CB A:PHE85 3.7 32.8 1.0 C A:ASN87 3.7 39.6 1.0 CB A:ALA137 3.8 25.7 1.0 N A:ASP86 3.9 35.7 1.0 CB A:SER136 4.1 26.3 1.0 CA A:ASN87 4.2 38.8 1.0 CG A:ASN87 4.3 37.8 1.0 CA A:SER136 4.3 25.8 1.0 CA A:ALA137 4.4 25.9 1.0 CD2 A:PHE85 4.4 31.2 1.0 C A:SER136 4.5 25.8 1.0 CG2 A:VAL93 4.6 30.7 1.0 CG A:PHE85 4.6 32.5 1.0 C A:ASP86 4.6 37.1 1.0 CA A:ASP86 4.7 36.5 1.0 N A:GLY88 4.8 40.4 1.0 CB A:ASN87 4.9 38.7 1.0

Iodine binding site 5 out of 44 in the Crystal Structures of the Interacting Domains From Yeast Glutamyl-Trna Synthetase and Trna Aminoacylation and Nuclear Export Cofactor ARC1P Reveal A Novel Function For An Old Fold


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 5 of Crystal Structures of the Interacting Domains From Yeast Glutamyl-Trna Synthetase and Trna Aminoacylation and Nuclear Export Cofactor ARC1P Reveal A Novel Function For An Old Fold within 5.0Å range: probe atom residue distance (Å) B Occ A:I408 b:36.6 occ:0.40 OE1 A:GLU117 3.6 37.2 1.0 CD A:LYS159 3.9 28.4 1.0 O A:HOH472 4.1 25.5 1.0 O A:HOH493 4.1 58.4 1.0 CB A:LYS159 4.2 23.8 1.0 CD A:GLU117 4.5 37.6 1.0 CG A:LYS159 4.6 24.5 1.0 O A:LYS159 4.7 23.6 1.0 CG A:GLU117 4.7 31.5 1.0 CE A:LYS159 4.8 27.7 1.0 CB A:GLU117 4.8 29.3 1.0

Iodine binding site 6 out of 44 in the Crystal Structures of the Interacting Domains From Yeast Glutamyl-Trna Synthetase and Trna Aminoacylation and Nuclear Export Cofactor ARC1P Reveal A Novel Function For An Old Fold


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 6 of Crystal Structures of the Interacting Domains From Yeast Glutamyl-Trna Synthetase and Trna Aminoacylation and Nuclear Export Cofactor ARC1P Reveal A Novel Function For An Old Fold within 5.0Å range: probe atom residue distance (Å) B Occ A:I411 b:47.1 occ:0.45 CG B:PRO30 3.8 29.3 1.0 CB A:MET151 4.1 33.5 1.0 CA A:MET151 4.1 33.4 1.0 N A:MET151 4.3 33.9 1.0 O A:HOH592 4.5 42.8 1.0 CG A:MET151 4.5 34.3 1.0 NZ A:LYS107 4.6 38.9 1.0 CD A:LYS107 4.7 36.3 1.0 C A:GLY150 4.7 33.9 1.0 CB B:PRO30 4.8 29.3 1.0 CD B:PRO30 4.8 29.5 1.0 SD A:MET151 4.9 38.1 1.0 O A:GLY150 4.9 33.9 1.0 CB B:LYS59 5.0 37.4 1.0 CE A:LYS107 5.0 37.9 1.0

Iodine binding site 7 out of 44 in the Crystal Structures of the Interacting Domains From Yeast Glutamyl-Trna Synthetase and Trna Aminoacylation and Nuclear Export Cofactor ARC1P Reveal A Novel Function For An Old Fold


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 7 of Crystal Structures of the Interacting Domains From Yeast Glutamyl-Trna Synthetase and Trna Aminoacylation and Nuclear Export Cofactor ARC1P Reveal A Novel Function For An Old Fold within 5.0Å range: probe atom residue distance (Å) B Occ A:I412 b:41.6 occ:0.40 ND2 A:ASN158 3.3 25.2 1.0 CB A:SER154 3.7 28.2 1.0 O A:SER154 3.7 29.5 1.0 CE1 A:PHE109 3.8 33.3 1.0 C A:SER154 3.8 28.2 1.0 CB B:LYS60 3.9 35.4 1.0 CD B:LYS60 4.0 36.8 1.0 CB A:ASN158 4.1 24.8 1.0 N A:ILE155 4.1 27.7 1.0 CG A:ASN158 4.1 26.2 1.0 CZ A:PHE109 4.2 32.2 1.0 CA A:ILE155 4.3 26.4 1.0 CG1 A:ILE155 4.3 26.3 1.0 CA A:SER154 4.4 28.7 1.0 CG B:LYS60 4.5 35.7 1.0 CA B:LYS60 4.7 34.9 1.0 O B:LYS60 4.8 33.8 1.0 OG A:SER154 4.9 31.4 1.0 CD1 A:PHE109 4.9 31.9 1.0 CB A:ILE155 5.0 25.9 1.0

Iodine binding site 8 out of 44 in the Crystal Structures of the Interacting Domains From Yeast Glutamyl-Trna Synthetase and Trna Aminoacylation and Nuclear Export Cofactor ARC1P Reveal A Novel Function For An Old Fold


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 8 of Crystal Structures of the Interacting Domains From Yeast Glutamyl-Trna Synthetase and Trna Aminoacylation and Nuclear Export Cofactor ARC1P Reveal A Novel Function For An Old Fold within 5.0Å range: probe atom residue distance (Å) B Occ A:I413 b:36.2 occ:0.30 O B:HOH540 3.6 38.7 1.0 CD A:LYS59 3.6 36.6 1.0 CE A:LYS59 3.6 37.1 1.0 CB B:SER154 4.1 30.9 1.0 NZ A:LYS59 4.1 33.7 1.0 CE A:LYS60 4.3 37.6 1.0 CG A:LYS60 4.3 34.4 1.0 CA B:MET151 4.5 34.6 1.0 OG B:SER154 4.5 34.2 1.0 O B:GLY150 4.6 33.4 1.0 CG A:LYS59 4.6 35.2 1.0 O B:MET151 4.8 34.0 1.0 CB A:LYS59 4.9 34.7 1.0 CD A:LYS60 5.0 36.6 1.0

Iodine binding site 9 out of 44 in the Crystal Structures of the Interacting Domains From Yeast Glutamyl-Trna Synthetase and Trna Aminoacylation and Nuclear Export Cofactor ARC1P Reveal A Novel Function For An Old Fold


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 9 of Crystal Structures of the Interacting Domains From Yeast Glutamyl-Trna Synthetase and Trna Aminoacylation and Nuclear Export Cofactor ARC1P Reveal A Novel Function For An Old Fold within 5.0Å range: probe atom residue distance (Å) B Occ A:I416 b:49.6 occ:0.40 O A:HOH554 2.7 60.0 1.0 N A:THR70 3.5 29.7 1.0 N A:GLU71 3.6 31.0 1.0 CA A:ALA69 3.7 30.4 1.0 CB A:GLU71 3.8 33.0 1.0 CB A:ALA69 4.0 30.0 1.0 C A:ALA69 4.1 29.5 1.0 OG1 A:THR70 4.1 27.3 1.0 CA A:GLU71 4.3 32.4 1.0 CA A:THR70 4.5 29.1 1.0 C A:THR70 4.5 30.0 1.0 O A:GLU71 4.6 33.2 1.0 OE1 A:GLU71 4.6 43.0 1.0 NZ A:LYS76 4.7 29.1 1.0 O A:ASP68 4.8 33.1 1.0 CE A:LYS76 4.9 32.3 1.0 N A:ALA69 4.9 30.8 1.0 C A:GLU71 4.9 32.4 1.0 CB A:THR70 5.0 29.6 1.0 CG A:GLU71 5.0 36.2 1.0

Iodine binding site 10 out of 44 in the Crystal Structures of the Interacting Domains From Yeast Glutamyl-Trna Synthetase and Trna Aminoacylation and Nuclear Export Cofactor ARC1P Reveal A Novel Function For An Old Fold


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 10 of Crystal Structures of the Interacting Domains From Yeast Glutamyl-Trna Synthetase and Trna Aminoacylation and Nuclear Export Cofactor ARC1P Reveal A Novel Function For An Old Fold within 5.0Å range: probe atom residue distance (Å) B Occ A:I418 b:34.9 occ:0.25 O A:HOH563 2.8 53.9 1.0 O A:HOH483 3.1 32.4 1.0 ND2 A:ASN44 3.3 25.5 1.0 CD1 A:ILE53 3.7 33.8 1.0 CB A:ASN44 3.9 25.0 1.0 CG A:ASN44 4.1 25.8 1.0 CG A:ARG41 4.2 27.1 1.0 CA A:ARG41 4.2 25.5 1.0 O A:ALA40 4.6 25.9 1.0 CB A:ARG41 4.7 25.4 1.0 CG1 A:ILE53 4.7 32.6 1.0 N A:ARG41 4.8 26.0 1.0 I A:IOD428 5.0 43.3 0.2 C A:ALA40 5.0 25.8 1.0

H.Simader, M.Hothorn, D.Suck. Structures of the Interacting Domains From Yeast Glutamyl-Trna Synthetase and Trna-Aminoacylation and Nuclear-Export Cofactor ARC1P Reveal A Novel Function For An Old Fold. Acta Crystallogr.,Sect.D V. 62 1510 2006.
ISSN: ISSN 0907-4449
PubMed: 17139087
DOI: 10.1107/S0907444906039850