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Zinc in PDB 2xs7: Crystal Structure of the Rrm Domain of Mouse Deleted in Azoospermia-Like in Complex with SYCP3 Rna, Uuguuu

Protein crystallography data

The structure of Crystal Structure of the Rrm Domain of Mouse Deleted in Azoospermia-Like in Complex with SYCP3 Rna, Uuguuu, PDB code: 2xs7 was solved by H.T.Jenkins, T.A.Edwards, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.83 / 1.45
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 32.888, 37.749, 70.771, 90.00, 90.00, 90.00
R / Rfree (%) 16.207 / 20.469

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Rrm Domain of Mouse Deleted in Azoospermia-Like in Complex with SYCP3 Rna, Uuguuu (pdb code 2xs7). 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 the Rrm Domain of Mouse Deleted in Azoospermia-Like in Complex with SYCP3 Rna, Uuguuu, PDB code: 2xs7:

Zinc binding site 1 out of 1 in 2xs7

Go back to Zinc Binding Sites List in 2xs7
Zinc binding site 1 out of 1 in the Crystal Structure of the Rrm Domain of Mouse Deleted in Azoospermia-Like in Complex with SYCP3 Rna, Uuguuu


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 Rrm Domain of Mouse Deleted in Azoospermia-Like in Complex with SYCP3 Rna, Uuguuu within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1118

b:15.8
occ:1.00
OE1 A:GLU55 1.9 17.8 1.0
O A:HOH2086 2.0 14.6 1.0
NE2 A:HIS104 2.1 20.2 1.0
CD A:GLU55 2.7 16.2 1.0
OE2 A:GLU55 2.8 17.2 1.0
CD2 A:HIS104 3.0 23.6 1.0
CE1 A:HIS104 3.1 22.9 1.0
CG A:GLU55 4.1 14.3 1.0
ND1 A:HIS104 4.2 24.3 1.0
CG A:HIS104 4.2 26.5 1.0
CB A:PHE103 4.4 29.2 1.0
O A:HOH2025 4.9 20.3 1.0
CG A:PHE103 5.0 30.2 1.0

Reference:

H.T.Jenkins, T.A.Edwards. Kinked Beta-Strands Mediate High-Affinity Recognition of Mrna Targets By the Germ-Cell Regulator Dazl Proc.Natl.Acad.Sci.Usa V. 108 18266 2011.
ISSN: ISSN 0027-8424
PubMed: 22021443
DOI: 10.1073/PNAS.1105211108
Page generated: Wed Dec 16 04:00:34 2020

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