Zinc in PDB 3a32: Crystal Structure of Putative Threonyl-Trna Synthetase Thrrs-1 From Aeropyrum Pernix

All present enzymatic activity of Crystal Structure of Putative Threonyl-Trna Synthetase Thrrs-1 From Aeropyrum Pernix:
6.1.1.3;

The structure of Crystal Structure of Putative Threonyl-Trna Synthetase Thrrs-1 From Aeropyrum Pernix, PDB code: 3a32 was solved by S.Shimizu, E.C.M.Juan, Y.Miyashita, Y.Sato, M.M.Hoque, K.Suzuki, M.Yogiashi, M.Tsunoda, A.-C.Dock-Bregeon, D.Moras, T.Sekiguchi, A.Takenaka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.30 / 2.30
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	81.486, 103.710, 112.537, 90.00, 90.00, 90.00
R / Rfree (%)	18 / 24

The binding sites of Zinc atom in the Crystal Structure of Putative Threonyl-Trna Synthetase Thrrs-1 From Aeropyrum Pernix (pdb code 3a32). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Putative Threonyl-Trna Synthetase Thrrs-1 From Aeropyrum Pernix, PDB code: 3a32:

Zinc binding site 1 out of 1 in the Crystal Structure of Putative Threonyl-Trna Synthetase Thrrs-1 From Aeropyrum Pernix


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 Putative Threonyl-Trna Synthetase Thrrs-1 From Aeropyrum Pernix within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn708 b:11.7 occ:1.00 NE2 A:HIS166 2.0 6.5 1.0 O A:HOH661 2.0 15.1 1.0 ND1 A:HIS310 2.1 9.6 1.0 SG A:CYS112 2.3 9.2 1.0 CE1 A:HIS166 2.9 5.6 1.0 CE1 A:HIS310 2.9 8.1 1.0 CD2 A:HIS166 3.1 7.8 1.0 CG A:HIS310 3.2 8.8 1.0 CB A:CYS112 3.2 6.8 1.0 CB A:HIS310 3.6 6.8 1.0 O2 A:SO4475 4.0 67.9 1.0 ND1 A:HIS166 4.0 8.7 1.0 CA A:CYS112 4.0 7.1 1.0 NE2 A:HIS310 4.1 8.9 1.0 CG A:HIS166 4.1 9.4 1.0 OD1 A:ASP164 4.2 11.4 1.0 N A:CYS112 4.2 6.6 1.0 CD2 A:HIS310 4.2 9.5 1.0 O A:HOH488 4.2 11.6 1.0 OD2 A:ASP164 4.4 13.9 1.0 CA A:HIS310 4.4 6.6 1.0 O A:HOH619 4.5 33.4 1.0 O A:HOH532 4.7 15.8 1.0 CG A:ASP164 4.7 10.4 1.0

S.Shimizu, E.C.M.Juan, Y.Sato, Y.Miyashita, M.M.Hoque, K.Suzuki, T.Sagara, M.Tsunoda, T.Sekiguchi, A.-C.Dock-Bregeon, D.Moras, A.Takenaka. Two Complementary Enzymes For Threonylation of Trna in Crenarchaeota: Crystal Structure of Aeropyrum Pernix Threonyl-Trna Synthetase Lacking A Cis-Editing Domain J.Mol.Biol. V. 394 286 2009.
ISSN: ISSN 0022-2836
PubMed: 19761773
DOI: 10.1016/J.JMB.2009.09.018