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Zinc in PDB 3a31: Crystal Structure of Putative Threonyl-Trna Synthetase Thrrs-1 From Aeropyrum Pernix (Selenomethionine Derivative)

Enzymatic activity of Crystal Structure of Putative Threonyl-Trna Synthetase Thrrs-1 From Aeropyrum Pernix (Selenomethionine Derivative)

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

Protein crystallography data

The structure of Crystal Structure of Putative Threonyl-Trna Synthetase Thrrs-1 From Aeropyrum Pernix (Selenomethionine Derivative), PDB code: 3a31 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) 41.00 / 2.50
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 82.000, 103.700, 112.700, 90.00, 90.00, 90.00
R / Rfree (%) 17 / 24

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Putative Threonyl-Trna Synthetase Thrrs-1 From Aeropyrum Pernix (Selenomethionine Derivative) (pdb code 3a31). 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 (Selenomethionine Derivative), PDB code: 3a31:

Zinc binding site 1 out of 1 in 3a31

Go back to Zinc Binding Sites List in 3a31
Zinc binding site 1 out of 1 in the Crystal Structure of Putative Threonyl-Trna Synthetase Thrrs-1 From Aeropyrum Pernix (Selenomethionine Derivative)


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 (Selenomethionine Derivative) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn743

b:28.1
occ:1.00
 NE2 A:HIS166 2.0 14.7 1.0
ND1 A:HIS310 2.0 19.1 1.0
SG A:CYS112 2.4 25.1 1.0
CE1 A:HIS166 2.8 13.2 1.0
CE1 A:HIS310 2.8 17.8 1.0
CG A:HIS310 3.1 14.7 1.0
CD2 A:HIS166 3.1 13.4 1.0
CB A:CYS112 3.2 18.4 1.0
CB A:HIS310 3.6 11.8 1.0
ND1 A:HIS166 4.0 12.8 1.0
NE2 A:HIS310 4.0 17.1 1.0
CA A:CYS112 4.0 18.8 1.0
CD2 A:HIS310 4.1 15.2 1.0
CG A:HIS166 4.2 14.1 1.0
N A:CYS112 4.2 19.0 1.0
O A:HOH487 4.3 24.9 1.0
OD1 A:ASP164 4.3 25.7 1.0
OD2 A:ASP164 4.3 27.3 1.0
CA A:HIS310 4.4 13.9 1.0
O A:HOH641 4.5 33.5 1.0
CG A:ASP164 4.7 24.0 1.0
O A:HOH582 4.9 31.0 1.0
O A:HOH534 5.0 34.0 1.0

Reference:

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
Page generated: Thu Oct 24 11:01:33 2024

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