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Zinc in PDB 4h3s: The Structure of Glutaminyl-Trna Synthetase From Saccharomyces Cerevisiae

Enzymatic activity of The Structure of Glutaminyl-Trna Synthetase From Saccharomyces Cerevisiae

All present enzymatic activity of The Structure of Glutaminyl-Trna Synthetase From Saccharomyces Cerevisiae:
6.1.1.18;

Protein crystallography data

The structure of The Structure of Glutaminyl-Trna Synthetase From Saccharomyces Cerevisiae, PDB code: 4h3s was solved by E.H.Snell, T.D.Grant, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 52.49 / 2.15
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 176.611, 176.611, 72.188, 90.00, 90.00, 120.00
R / Rfree (%) 16 / 17.6

Other elements in 4h3s:

The structure of The Structure of Glutaminyl-Trna Synthetase From Saccharomyces Cerevisiae also contains other interesting chemical elements:

Bromine (Br) 1 atom
Chlorine (Cl) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the The Structure of Glutaminyl-Trna Synthetase From Saccharomyces Cerevisiae (pdb code 4h3s). 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 The Structure of Glutaminyl-Trna Synthetase From Saccharomyces Cerevisiae, PDB code: 4h3s:

Zinc binding site 1 out of 1 in 4h3s

Go back to Zinc Binding Sites List in 4h3s
Zinc binding site 1 out of 1 in the The Structure of Glutaminyl-Trna Synthetase From Saccharomyces Cerevisiae


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Structure of Glutaminyl-Trna Synthetase From Saccharomyces Cerevisiae within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn901

b:40.4
occ:1.00
 ND1 A:HIS374 2.0 39.1 1.0
SG A:CYS346 2.3 38.4 1.0
SG A:CYS372 2.3 37.2 1.0
SG A:CYS348 2.4 38.6 1.0
CE1 A:HIS374 2.9 39.4 1.0
HB2 A:HIS374 3.0 44.8 1.0
HE1 A:HIS374 3.0 47.3 1.0
HB2 A:CYS372 3.0 56.1 1.0
CG A:HIS374 3.1 38.2 1.0
H A:CYS348 3.1 51.1 1.0
CB A:CYS372 3.2 46.8 1.0
HB2 A:CYS348 3.2 42.7 1.0
H A:HIS347 3.3 45.7 1.0
HB3 A:CYS372 3.3 56.1 1.0
CB A:CYS348 3.4 35.6 1.0
CB A:CYS346 3.5 41.1 1.0
HA A:CYS346 3.5 46.5 1.0
CB A:HIS374 3.6 37.3 1.0
HB2 A:CYS346 3.6 49.3 1.0
N A:CYS348 3.7 42.6 1.0
H A:HIS374 3.8 46.6 1.0
N A:HIS347 3.9 38.1 1.0
HE2 A:TYR344 3.9 45.1 1.0
HH11 A:ARG402 3.9 41.5 1.0
CA A:CYS346 4.0 38.7 1.0
O A:HOH1222 4.0 47.9 1.0
NE2 A:HIS374 4.0 38.2 1.0
CA A:CYS348 4.1 39.3 1.0
HB3 A:HIS374 4.2 44.8 1.0
CD2 A:HIS374 4.2 38.3 1.0
HB3 A:CYS348 4.2 42.7 1.0
HB3 A:CYS346 4.3 49.3 1.0
C A:CYS346 4.3 38.4 1.0
HA A:CYS348 4.4 47.1 1.0
N A:HIS374 4.5 38.8 1.0
C A:HIS347 4.6 43.0 1.0
CA A:CYS372 4.6 42.3 1.0
NH1 A:ARG402 4.6 34.5 1.0
CA A:HIS374 4.6 37.9 1.0
HH12 A:ARG402 4.7 41.5 1.0
HE2 A:HIS374 4.8 45.9 1.0
O A:HOH1133 4.8 38.6 1.0
CE2 A:TYR344 4.8 37.6 1.0
CA A:HIS347 4.9 40.3 1.0
HD3 A:ARG402 4.9 46.2 1.0
H A:CYS372 4.9 49.6 1.0
H A:LYS373 5.0 52.5 1.0

Reference:

T.D.Grant, J.R.Luft, J.R.Wolfley, M.E.Snell, H.Tsuruta, S.Corretore, E.Quartley, E.M.Phizicky, E.J.Grayhack, E.H.Snell. The Structure of Yeast Glutaminyl-Trna Synthetase and Modeling of Its Interaction with Trna. J.Mol.Biol. V. 425 2480 2013.
ISSN: ISSN 0022-2836
PubMed: 23583912
DOI: 10.1016/J.JMB.2013.03.043
Page generated: Sat Oct 26 23:52:47 2024

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