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Zinc in PDB 2oaj: Crystal Structure of SRO7 From S. Cerevisiae

Protein crystallography data

The structure of Crystal Structure of SRO7 From S. Cerevisiae, PDB code: 2oaj was solved by D.A.Hattendorf, W.I.Weis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.12 / 2.40
Space group P 4 21 2
Cell size a, b, c (Å), α, β, γ (°) 130.520, 130.520, 116.023, 90.00, 90.00, 90.00
R / Rfree (%) 21.1 / 26.2

Other elements in 2oaj:

The structure of Crystal Structure of SRO7 From S. Cerevisiae also contains other interesting chemical elements:

Sodium (Na) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of SRO7 From S. Cerevisiae (pdb code 2oaj). 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 Crystal Structure of SRO7 From S. Cerevisiae, PDB code: 2oaj:

Zinc binding site 1 out of 1 in 2oaj

Go back to Zinc Binding Sites List in 2oaj
Zinc binding site 1 out of 1 in the Crystal Structure of SRO7 From S. Cerevisiae


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 SRO7 From S. Cerevisiae within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn963

b:32.2
occ:1.00
ND1 A:HIS835 2.3 27.9 1.0
ND1 A:HIS851 2.3 22.7 1.0
O A:HOH1220 2.4 7.5 1.0
O A:HOH1219 2.5 14.0 1.0
CG A:HIS835 3.2 26.1 1.0
CE1 A:HIS835 3.2 28.5 1.0
CG A:HIS851 3.2 26.2 1.0
CE1 A:HIS851 3.3 25.5 1.0
CB A:HIS835 3.4 21.4 1.0
CB A:HIS851 3.4 24.5 1.0
CA A:HIS835 4.2 21.2 1.0
CD2 A:HIS835 4.3 28.0 1.0
NE2 A:HIS835 4.3 30.0 1.0
CA A:HIS851 4.3 25.4 1.0
CD2 A:HIS851 4.4 27.2 1.0
NE2 A:HIS851 4.4 29.1 1.0
ND2 A:ASN833 4.6 13.3 1.0
N A:HIS851 4.7 28.1 1.0
N A:HIS835 4.7 19.4 1.0
O A:HOH1097 4.9 23.3 1.0

Reference:

D.A.Hattendorf, A.Andreeva, A.Gangar, P.J.Brennwald, W.I.Weis. Structure of the Yeast Polarity Protein SRO7 Reveals A Snare Regulatory Mechanism. Nature V. 446 567 2007.
ISSN: ISSN 0028-0836
PubMed: 17392788
DOI: 10.1038/NATURE05635
Page generated: Wed Dec 16 03:45:41 2020

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