Zinc in PDB 4ttv: Crystal Structure of Human Thrrs Complexing with A Bioengineered Macrolide BC194

All present enzymatic activity of Crystal Structure of Human Thrrs Complexing with A Bioengineered Macrolide BC194:
6.1.1.3;

The structure of Crystal Structure of Human Thrrs Complexing with A Bioengineered Macrolide BC194, PDB code: 4ttv was solved by P.Fang, M.Guo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.51 / 2.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	92.020, 134.610, 128.670, 90.00, 90.10, 90.00
R / Rfree (%)	25.5 / 28.8

The binding sites of Zinc atom in the Crystal Structure of Human Thrrs Complexing with A Bioengineered Macrolide BC194 (pdb code 4ttv). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of Human Thrrs Complexing with A Bioengineered Macrolide BC194, PDB code: 4ttv:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Crystal Structure of Human Thrrs Complexing with A Bioengineered Macrolide BC194


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Human Thrrs Complexing with A Bioengineered Macrolide BC194 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn802 b:71.4 occ:1.00 NE2 A:HIS464 2.2 34.8 1.0 ND1 A:HIS590 2.3 39.7 1.0 SG A:CYS413 2.5 33.0 1.0 CE1 A:HIS464 3.0 35.6 1.0 CD2 A:HIS464 3.1 36.0 1.0 CG A:HIS590 3.2 39.1 1.0 CE1 A:HIS590 3.3 40.0 1.0 CB A:HIS590 3.4 37.8 1.0 OD1 A:ASP462 3.9 43.3 1.0 CB A:CYS413 3.9 41.7 1.0 ND1 A:HIS464 4.0 36.3 1.0 CG A:HIS464 4.1 36.6 1.0 CA A:HIS590 4.1 37.8 1.0 OD2 A:ASP462 4.2 43.4 1.0 C7 A:BC9801 4.3 45.6 1.0 O A:HOH910 4.3 45.6 1.0 CD2 A:HIS590 4.3 40.0 1.0 NE2 A:HIS590 4.4 40.3 1.0 CG A:ASP462 4.5 43.2 1.0 C5 A:BC9801 4.5 47.9 1.0 CA A:CYS413 4.6 42.2 1.0 C9 A:BC9801 4.6 45.8 1.0 N A:CYS413 4.7 42.3 1.0 C8 A:BC9801 4.9 45.4 1.0 C1 A:BC9801 5.0 47.2 1.0

Zinc binding site 2 out of 4 in the Crystal Structure of Human Thrrs Complexing with A Bioengineered Macrolide BC194


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Human Thrrs Complexing with A Bioengineered Macrolide BC194 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn802 b:58.0 occ:1.00 NE2 B:HIS464 2.2 45.8 1.0 ND1 B:HIS590 2.2 42.3 1.0 SG B:CYS413 2.5 35.9 1.0 CE1 B:HIS464 2.9 45.4 1.0 CD2 B:HIS464 3.1 46.0 1.0 CE1 B:HIS590 3.1 42.2 1.0 CG B:HIS590 3.2 42.9 1.0 CB B:HIS590 3.5 43.2 1.0 CB B:CYS413 3.8 46.8 1.0 OD1 B:ASP462 3.9 50.1 1.0 ND1 B:HIS464 3.9 45.0 1.0 CG B:HIS464 4.1 45.2 1.0 OD2 B:ASP462 4.1 48.6 1.0 CA B:HIS590 4.2 43.3 1.0 NE2 B:HIS590 4.3 43.3 1.0 O B:HOH906 4.3 51.9 1.0 C7 B:BC9801 4.3 52.3 1.0 CD2 B:HIS590 4.3 43.7 1.0 CA B:CYS413 4.4 45.7 1.0 C9 B:BC9801 4.4 51.5 1.0 CG B:ASP462 4.5 48.8 1.0 C5 B:BC9801 4.5 52.4 1.0 N B:CYS413 4.5 45.2 1.0 C8 B:BC9801 4.8 52.3 1.0 C1 B:BC9801 4.9 52.6 1.0

Zinc binding site 3 out of 4 in the Crystal Structure of Human Thrrs Complexing with A Bioengineered Macrolide BC194


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Human Thrrs Complexing with A Bioengineered Macrolide BC194 within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn802 b:65.5 occ:1.00 NE2 C:HIS464 2.2 46.5 1.0 ND1 C:HIS590 2.2 42.1 1.0 SG C:CYS413 2.5 37.8 1.0 CE1 C:HIS464 2.9 46.1 1.0 CG C:HIS590 3.1 43.0 1.0 CD2 C:HIS464 3.2 46.8 1.0 CE1 C:HIS590 3.3 42.4 1.0 CB C:HIS590 3.3 43.1 1.0 CB C:CYS413 3.9 48.7 1.0 OD1 C:ASP462 3.9 52.3 1.0 ND1 C:HIS464 4.0 46.0 1.0 CG C:HIS464 4.1 46.5 1.0 CA C:HIS590 4.1 43.3 1.0 OD2 C:ASP462 4.2 50.3 1.0 C7 C:BC9801 4.2 50.0 1.0 C9 C:BC9801 4.3 49.8 1.0 CD2 C:HIS590 4.3 44.0 1.0 NE2 C:HIS590 4.3 43.7 1.0 C5 C:BC9801 4.4 50.4 1.0 CG C:ASP462 4.5 50.3 1.0 CA C:CYS413 4.5 47.3 1.0 C8 C:BC9801 4.6 50.3 1.0 N C:CYS413 4.7 47.2 1.0 C1 C:BC9801 4.9 50.5 1.0

Zinc binding site 4 out of 4 in the Crystal Structure of Human Thrrs Complexing with A Bioengineered Macrolide BC194


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Human Thrrs Complexing with A Bioengineered Macrolide BC194 within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn802 b:61.0 occ:1.00 NE2 D:HIS464 2.1 44.0 1.0 ND1 D:HIS590 2.3 43.0 1.0 SG D:CYS413 2.5 38.1 1.0 CE1 D:HIS464 2.9 44.4 1.0 CD2 D:HIS464 3.2 44.7 1.0 CG D:HIS590 3.2 42.1 1.0 CE1 D:HIS590 3.2 43.4 1.0 CB D:HIS590 3.4 40.2 1.0 C8 D:BC9801 3.8 47.4 1.0 CB D:CYS413 3.9 43.2 1.0 C9 D:BC9801 4.1 47.6 1.0 OD1 D:ASP462 4.1 49.9 1.0 ND1 D:HIS464 4.1 45.0 1.0 OD2 D:ASP462 4.2 49.8 1.0 CG D:HIS464 4.2 45.1 1.0 CA D:HIS590 4.3 39.3 1.0 CD2 D:HIS590 4.3 43.1 1.0 NE2 D:HIS590 4.3 43.4 1.0 CA D:CYS413 4.5 43.3 1.0 C5 D:BC9801 4.5 48.9 1.0 O D:HOH909 4.5 52.1 1.0 CG D:ASP462 4.6 49.5 1.0 N D:CYS413 4.6 43.5 1.0 C7 D:BC9801 4.9 47.3 1.0

A.C.Mirando, P.Fang, T.F.Williams, L.C.Baldor, A.K.Howe, A.M.Ebert, B.Wilkinson, K.M.Lounsbury, M.Guo, C.S.Francklyn. Aminoacyl-Trna Synthetase Dependent Angiogenesis Revealed By A Bioengineered Macrolide Inhibitor. Sci Rep V. 5 13160 2015.
ISSN: ESSN 2045-2322
PubMed: 26271225
DOI: 10.1038/SREP13160