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Zinc in PDB 3pdh: Structure of SIR2TM Bound to A Propionylated Peptide

Protein crystallography data

The structure of Structure of SIR2TM Bound to A Propionylated Peptide, PDB code: 3pdh was solved by C.Wolberger, P.Bheda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.01 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.561, 60.013, 106.345, 90.00, 90.00, 90.00
R / Rfree (%) 16.5 / 21

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of SIR2TM Bound to A Propionylated Peptide (pdb code 3pdh). 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 Structure of SIR2TM Bound to A Propionylated Peptide, PDB code: 3pdh:

Zinc binding site 1 out of 1 in 3pdh

Go back to Zinc Binding Sites List in 3pdh
Zinc binding site 1 out of 1 in the Structure of SIR2TM Bound to A Propionylated Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of SIR2TM Bound to A Propionylated Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1001

b:20.7
occ:1.00
SG A:CYS127 2.2 23.0 1.0
SG A:CYS148 2.3 22.9 1.0
SG A:CYS151 2.3 22.1 1.0
SG A:CYS124 2.4 17.1 1.0
CB A:CYS148 3.0 21.1 1.0
CB A:CYS124 3.1 18.3 1.0
CB A:CYS127 3.4 23.6 1.0
CB A:CYS151 3.6 30.1 1.0
N A:CYS151 3.8 29.6 1.0
N A:CYS127 3.9 20.0 1.0
CA A:CYS127 4.2 22.3 1.0
CA A:CYS151 4.2 30.0 1.0
CA A:CYS148 4.5 21.6 1.0
CA A:CYS124 4.6 15.1 1.0
CB A:ASP150 4.7 33.4 1.0
C A:CYS151 4.7 29.6 1.0
CB A:SER153 4.7 20.9 1.0
N A:SER153 4.7 21.9 1.0
CB A:LYS129 4.7 23.0 1.0
N A:ASN152 4.8 27.8 1.0
C A:CYS127 4.8 22.4 1.0
CB A:ARG126 4.8 20.3 1.0
O A:HOH325 4.8 35.7 1.0
C A:ASP150 4.8 31.7 1.0
N A:GLU128 4.9 18.3 1.0
OG A:SER153 4.9 22.4 1.0
C A:ARG126 5.0 20.7 1.0

Reference:

P.Bheda, J.T.Wang, J.C.Escalante-Semerena, C.Wolberger. Structure of SIR2TM Bound to A Propionylated Peptide. Protein Sci. V. 20 131 2011.
ISSN: ISSN 0961-8368
PubMed: 21080423
DOI: 10.1002/PRO.544
Page generated: Wed Dec 16 04:42:54 2020

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