Calcium in PDB 2d3d: Crystal Structure of the Rna Binding Sam Domain of Saccharomyces Cerevisiae VTS1

The structure of Crystal Structure of the Rna Binding Sam Domain of Saccharomyces Cerevisiae VTS1, PDB code: 2d3d was solved by T.Aviv, A.N.Amborski, X.S.Zhao, J.J.Kwan, P.E.Johnson, F.Sicheri, L.W.Donaldson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.60 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	27.380, 27.890, 99.910, 90.00, 90.00, 90.00
R / Rfree (%)	20.6 / 25.6

The binding sites of Calcium atom in the Crystal Structure of the Rna Binding Sam Domain of Saccharomyces Cerevisiae VTS1 (pdb code 2d3d). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of the Rna Binding Sam Domain of Saccharomyces Cerevisiae VTS1, PDB code: 2d3d:

Calcium binding site 1 out of 1 in the Crystal Structure of the Rna Binding Sam Domain of Saccharomyces Cerevisiae VTS1


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of the Rna Binding Sam Domain of Saccharomyces Cerevisiae VTS1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca101 b:18.7 occ:1.00 OH A:TYR468 2.9 15.6 1.0 O A:HOH37 3.1 29.2 1.0 N A:ALA495 3.2 12.3 1.0 N A:LEU494 3.3 12.0 1.0 CE1 A:TYR468 3.6 13.7 1.0 CZ A:TYR468 3.7 14.6 1.0 CB A:LEU494 3.7 13.1 1.0 CB A:ALA495 3.8 12.7 1.0 CA A:LEU494 3.8 12.5 1.0 C A:LEU494 3.9 12.5 1.0 CA A:ALA495 4.1 11.8 1.0 O A:GLY492 4.1 11.4 1.0 C A:VAL493 4.2 11.3 1.0 CG A:LEU494 4.4 13.7 1.0 CA A:VAL493 4.5 11.2 1.0 O A:HOH9 4.9 23.7 1.0 CD1 A:TYR468 4.9 14.4 1.0 CD1 A:LEU494 5.0 15.2 1.0

T.Aviv, A.N.Amborski, X.S.Zhao, J.J.Kwan, P.E.Johnson, F.Sicheri, L.W.Donaldson. The uc(Nmr) and X-Ray Structures of the Saccharomyces Cerevisiae VTS1 Sam Domain Define A Surface For the Recognition of Rna Hairpins J.Mol.Biol. V. 356 274 2006.
ISSN: ISSN 0022-2836
PubMed: 16375924
DOI: 10.1016/J.JMB.2005.11.066