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Zinc in PDB 3iqx: Adp Complex of C.Therm. GET3 in Closed Form

Protein crystallography data

The structure of Adp Complex of C.Therm. GET3 in Closed Form, PDB code: 3iqx was solved by G.Bozkurt, K.Wild, I.Sinning, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.28 / 3.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.750, 105.590, 137.350, 90.00, 90.00, 90.00
R / Rfree (%) 22.9 / 29.5

Other elements in 3iqx:

The structure of Adp Complex of C.Therm. GET3 in Closed Form also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Adp Complex of C.Therm. GET3 in Closed Form (pdb code 3iqx). 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 Adp Complex of C.Therm. GET3 in Closed Form, PDB code: 3iqx:

Zinc binding site 1 out of 1 in 3iqx

Go back to Zinc Binding Sites List in 3iqx
Zinc binding site 1 out of 1 in the Adp Complex of C.Therm. GET3 in Closed Form


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Adp Complex of C.Therm. GET3 in Closed Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn3

b:36.6
occ:1.00
SG A:CYS281 2.0 75.0 1.0
SG A:CYS284 2.1 63.7 1.0
SG B:CYS284 2.5 55.6 1.0
SG B:CYS281 2.9 61.4 1.0
N A:CYS284 3.1 66.0 1.0
CB A:CYS284 3.1 63.5 1.0
CB A:CYS281 3.3 76.9 1.0
CA A:CYS284 3.6 62.9 1.0
O A:CYS281 3.9 74.3 1.0
C A:GLN283 4.1 66.4 1.0
CB B:CYS281 4.1 65.0 1.0
CB A:GLN283 4.2 70.0 1.0
CB B:CYS284 4.2 56.6 1.0
C A:CYS281 4.3 78.3 1.0
CA A:CYS281 4.4 80.4 1.0
CA A:GLN283 4.5 70.2 1.0
N A:GLN283 4.5 74.3 1.0
N B:CYS284 4.8 56.7 1.0
C A:CYS284 4.9 63.2 1.0

Reference:

G.Bozkurt, G.Stjepanovic, F.Vilardi, S.Amlacher, K.Wild, G.Bange, V.Favaloro, K.Rippe, E.Hurt, B.Dobberstein, I.Sinning. Structural Insights Into Tail-Anchored Protein Binding and Membrane Insertion By GET3. Proc.Natl.Acad.Sci.Usa V. 106 21131 2009.
ISSN: ISSN 0027-8424
PubMed: 19948960
DOI: 10.1073/PNAS.0910223106
Page generated: Wed Dec 16 04:26:56 2020

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