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Zinc in PDB 4p3p: Structural Basis For Full-Spectrum Inhibition of Threonyl-Trna Synthetase By Borrelidin 3

Enzymatic activity of Structural Basis For Full-Spectrum Inhibition of Threonyl-Trna Synthetase By Borrelidin 3

All present enzymatic activity of Structural Basis For Full-Spectrum Inhibition of Threonyl-Trna Synthetase By Borrelidin 3:
6.1.1.3;

Protein crystallography data

The structure of Structural Basis For Full-Spectrum Inhibition of Threonyl-Trna Synthetase By Borrelidin 3, PDB code: 4p3p was solved by P.Fang, X.Yu, K.Chen, X.Chen, M.Guo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.80 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 94.534, 107.640, 109.623, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 21.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Structural Basis For Full-Spectrum Inhibition of Threonyl-Trna Synthetase By Borrelidin 3 (pdb code 4p3p). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structural Basis For Full-Spectrum Inhibition of Threonyl-Trna Synthetase By Borrelidin 3, PDB code: 4p3p:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 4p3p

Go back to Zinc Binding Sites List in 4p3p
Zinc binding site 1 out of 2 in the Structural Basis For Full-Spectrum Inhibition of Threonyl-Trna Synthetase By Borrelidin 3


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structural Basis For Full-Spectrum Inhibition of Threonyl-Trna Synthetase By Borrelidin 3 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:18.2
occ:1.00
NE2 A:HIS385 2.1 16.1 1.0
ND1 A:HIS511 2.2 14.5 1.0
O A:HOH934 2.3 19.2 1.0
SG A:CYS334 2.4 13.5 1.0
CE1 A:HIS511 3.0 14.7 1.0
CE1 A:HIS385 3.0 15.6 1.0
CB A:CYS334 3.1 13.7 1.0
CD2 A:HIS385 3.1 16.7 1.0
O A:HOH893 3.2 16.8 1.0
CG A:HIS511 3.4 15.1 1.0
CB A:HIS511 3.9 15.0 1.0
OD2 A:ASP383 4.0 19.1 1.0
CA A:CYS334 4.0 13.2 1.0
OD1 A:ASP383 4.1 19.6 1.0
C9 A:2CR702 4.1 17.1 1.0
N A:CYS334 4.1 12.8 1.0
ND1 A:HIS385 4.2 15.8 1.0
NE2 A:HIS511 4.2 15.3 1.0
O A:HOH888 4.2 14.2 1.0
CG A:HIS385 4.2 16.4 1.0
CD2 A:HIS511 4.4 15.5 1.0
CG A:ASP383 4.5 19.3 1.0
CA A:HIS511 4.7 15.1 1.0
C8 A:2CR702 4.8 17.5 1.0
C5 A:2CR702 4.9 16.9 1.0
C7 A:2CR702 5.0 17.5 1.0

Zinc binding site 2 out of 2 in 4p3p

Go back to Zinc Binding Sites List in 4p3p
Zinc binding site 2 out of 2 in the Structural Basis For Full-Spectrum Inhibition of Threonyl-Trna Synthetase By Borrelidin 3


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structural Basis For Full-Spectrum Inhibition of Threonyl-Trna Synthetase By Borrelidin 3 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn701

b:21.4
occ:1.00
ND1 B:HIS511 2.1 12.3 1.0
NE2 B:HIS385 2.1 15.1 1.0
SG B:CYS334 2.2 13.6 1.0
O B:HOH920 2.3 28.4 1.0
CE1 B:HIS511 2.7 12.5 1.0
CB B:CYS334 2.8 13.7 1.0
CD2 B:HIS385 3.1 15.3 1.0
CE1 B:HIS385 3.2 14.7 1.0
O B:HOH900 3.3 29.1 1.0
CG B:HIS511 3.3 12.8 1.0
CA B:CYS334 3.8 13.2 1.0
CB B:HIS511 3.9 12.7 1.0
NE2 B:HIS511 3.9 13.0 1.0
OD2 B:ASP383 4.0 19.8 1.0
N B:CYS334 4.1 12.9 1.0
O B:HOH865 4.1 21.8 1.0
C9 B:2CR702 4.1 16.7 1.0
OD1 B:ASP383 4.1 20.1 1.0
CG B:HIS385 4.2 15.0 1.0
CD2 B:HIS511 4.2 13.1 1.0
ND1 B:HIS385 4.3 14.5 1.0
CG B:ASP383 4.5 19.9 1.0
CA B:HIS511 4.7 12.7 1.0
C8 B:2CR702 4.8 17.1 1.0
C7 B:2CR702 4.9 17.1 1.0
C10 B:2CR702 5.0 17.0 1.0

Reference:

P.Fang, X.Yu, S.Jeong, A.Mirando, K.Chen, X.Chen, S.Kim, C.S.Francklyn, M.Guo. Structural Basis For Full-Spectrum Inhibition of Translational and Nontranslational Functions on A Human Trna Synthetase To Be Published.
Page generated: Sun Oct 27 04:12:37 2024

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