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Zinc in PDB 2hjh: Crystal Structure of the SIR2 Deacetylase

Protein crystallography data

The structure of Crystal Structure of the SIR2 Deacetylase, PDB code: 2hjh was solved by B.E.Hall, T.E.Ellenberger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.85
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 52.353, 89.566, 94.510, 90.00, 104.95, 90.00
R / Rfree (%) 17.1 / 21.5

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the SIR2 Deacetylase (pdb code 2hjh). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the SIR2 Deacetylase, PDB code: 2hjh:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2hjh

Go back to Zinc Binding Sites List in 2hjh
Zinc binding site 1 out of 2 in the Crystal Structure of the SIR2 Deacetylase


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 the SIR2 Deacetylase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn800

b:32.0
occ:1.00
SG A:CYS375 2.3 21.6 1.0
SG A:CYS396 2.3 21.8 1.0
SG A:CYS399 2.4 22.4 1.0
SG A:CYS372 2.4 20.8 1.0
CB A:CYS372 3.1 19.8 1.0
CB A:CYS396 3.1 20.5 1.0
CB A:CYS375 3.3 22.3 1.0
CB A:CYS399 3.4 22.2 1.0
N A:CYS375 3.8 23.4 1.0
N A:CYS399 3.8 22.2 1.0
CA A:CYS375 4.0 21.9 1.0
CA A:CYS399 4.2 22.8 1.0
CB A:TYR398 4.5 23.1 1.0
CA A:CYS372 4.6 20.0 1.0
CA A:CYS396 4.6 21.8 1.0
CB A:THR374 4.7 22.2 1.0
C A:TYR398 4.7 22.4 1.0
C A:CYS375 4.7 23.3 1.0
CA A:GLY436 4.8 19.4 1.0
CB A:TRP377 4.8 26.4 1.0
N A:HIS376 4.8 23.6 1.0
C A:THR374 4.9 23.1 1.0
CA A:TYR398 5.0 22.7 1.0
N A:TYR398 5.0 22.5 1.0

Zinc binding site 2 out of 2 in 2hjh

Go back to Zinc Binding Sites List in 2hjh
Zinc binding site 2 out of 2 in the Crystal Structure of the SIR2 Deacetylase


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 the SIR2 Deacetylase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn800

b:31.9
occ:1.00
SG B:CYS399 2.2 24.7 1.0
SG B:CYS396 2.3 22.7 1.0
SG B:CYS375 2.4 22.9 1.0
SG B:CYS372 2.4 22.0 1.0
CB B:CYS396 3.1 24.0 1.0
CB B:CYS372 3.2 21.1 1.0
CB B:CYS399 3.3 26.1 1.0
CB B:CYS375 3.3 23.0 1.0
N B:CYS375 3.7 23.1 1.0
N B:CYS399 3.9 25.2 1.0
CA B:CYS375 4.1 22.8 1.0
CA B:CYS399 4.1 26.3 1.0
CB B:TYR398 4.4 26.9 1.0
CA B:CYS396 4.6 23.9 1.0
C B:TYR398 4.6 26.3 1.0
CB B:THR374 4.6 23.5 1.0
CA B:CYS372 4.7 21.3 1.0
C B:CYS375 4.8 24.7 1.0
CA B:GLY436 4.8 31.4 1.0
C B:THR374 4.8 24.0 1.0
CB B:TRP377 4.8 27.9 1.0
N B:HIS376 4.9 25.8 1.0
CA B:TYR398 4.9 26.1 1.0

Reference:

B.E.Hall, J.R.Buchberger, S.A.Gerber, A.L.B.Ambrosio, S.P.Gygi, D.Filman, D.Moazed, T.Ellenberger. Autoregulation of the Yeast SIR2 Deacetylase By Reaction and Trapping of A Pseudosubstrate Motif in the Active Site To Be Published.
Page generated: Sat Sep 26 02:18:45 2020
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