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Zinc in PDB 4twi: The Structure of SIR2AF1 Bound to A Succinylated Histone Peptide

Protein crystallography data

The structure of The Structure of SIR2AF1 Bound to A Succinylated Histone Peptide, PDB code: 4twi was solved by A.E.Ringel, C.Roman, C.Wolberger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 21.94 / 1.79
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 44.610, 51.362, 57.687, 90.00, 101.85, 90.00
R / Rfree (%) 19.2 / 22.1

Zinc Binding Sites:

The binding sites of Zinc atom in the The Structure of SIR2AF1 Bound to A Succinylated Histone Peptide (pdb code 4twi). 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 SIR2AF1 Bound to A Succinylated Histone Peptide, PDB code: 4twi:

Zinc binding site 1 out of 1 in 4twi

Go back to Zinc Binding Sites List in 4twi
Zinc binding site 1 out of 1 in the The Structure of SIR2AF1 Bound to A Succinylated Histone Peptide


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 SIR2AF1 Bound to A Succinylated Histone Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:19.2
occ:1.00
SG A:CYS127 2.3 20.0 1.0
SG A:CYS145 2.3 19.5 1.0
SG A:CYS148 2.3 21.5 1.0
SG A:CYS124 2.4 14.9 1.0
CB A:CYS145 3.1 19.7 1.0
CB A:CYS124 3.2 14.9 1.0
CB A:CYS127 3.4 19.9 1.0
CB A:CYS148 3.4 22.2 1.0
N A:CYS148 3.8 23.3 1.0
N A:CYS127 3.9 19.3 1.0
CA A:CYS127 4.1 19.9 1.0
CA A:CYS148 4.2 22.3 1.0
CB A:ASN129 4.3 20.5 1.0
CA A:CYS124 4.6 14.9 1.0
CA A:CYS145 4.6 19.8 1.0
CB A:LYS147 4.6 25.7 1.0
CB A:SER150 4.7 18.4 1.0
C A:CYS127 4.7 20.4 1.0
O A:HOH408 4.7 30.2 1.0
C A:CYS148 4.8 21.8 1.0
N A:SER150 4.8 18.7 1.0
N A:GLY149 4.8 20.8 1.0
C A:LYS147 4.8 24.4 1.0
O A:CYS127 5.0 19.9 1.0

Reference:

A.E.Ringel, C.Roman, C.Wolberger. Alternate Deacylating Specificities of the Archaeal Sirtuins SIR2AF1 and SIR2AF2. Protein Sci. V. 23 1686 2014.
ISSN: ESSN 1469-896X
PubMed: 25200501
DOI: 10.1002/PRO.2546
Page generated: Wed Dec 16 05:47:23 2020

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