Samarium in PDB 1soi: Crystal Structure of Nudix Hydrolase DR1025 in Complex with Sm+3

The structure of Crystal Structure of Nudix Hydrolase DR1025 in Complex with Sm+3, PDB code: 1soi was solved by W.Ranatunga, E.E.Hill, J.L.Mooster, E.L.Holbrook, U.Schulze-Gahmen, W.Xu, M.J.Bessman, S.E.Brenner, S.R.Holbrook, Berkeleystructural Genomics Center (Bsgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.60 / 1.80
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	53.171, 53.171, 121.972, 90.00, 90.00, 90.00
R / Rfree (%)	21.8 / 25.1

The binding sites of Samarium atom in the Crystal Structure of Nudix Hydrolase DR1025 in Complex with Sm+3 (pdb code 1soi). This binding sites where shown within 5.0 Angstroms radius around Samarium atom.
In total 3 binding sites of Samarium where determined in the Crystal Structure of Nudix Hydrolase DR1025 in Complex with Sm+3, PDB code: 1soi:
Jump to Samarium binding site number: 1; 2; 3;

Samarium binding site 1 out of 3 in the Crystal Structure of Nudix Hydrolase DR1025 in Complex with Sm+3


Mono view


Stereo pair view

A full contact list of Samarium with other atoms in the Sm binding site number 1 of Crystal Structure of Nudix Hydrolase DR1025 in Complex with Sm+3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Sm301 b:28.5 occ:1.00 O A:HOH730 2.3 27.2 1.0 OE1 A:GLU65 2.4 13.7 1.0 OE2 A:GLU65 2.4 13.6 1.0 OE1 A:GLU68 2.4 29.1 1.0 O A:HOH772 2.5 17.6 1.0 CD A:GLU65 2.7 12.7 1.0 CD A:GLU68 3.3 26.9 1.0 OE2 A:GLU68 3.5 29.5 1.0 O A:HOH748 4.1 27.2 1.0 CG A:GLU65 4.3 11.4 1.0 NE A:ARG64 4.5 20.0 1.0 CG A:GLU68 4.8 25.7 1.0 O A:ALA51 4.9 12.7 1.0 NH2 A:ARG64 4.9 19.4 1.0

Samarium binding site 2 out of 3 in the Crystal Structure of Nudix Hydrolase DR1025 in Complex with Sm+3


Mono view


Stereo pair view

A full contact list of Samarium with other atoms in the Sm binding site number 2 of Crystal Structure of Nudix Hydrolase DR1025 in Complex with Sm+3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Sm302 b:32.7 occ:1.00 OD1 A:ASP147 2.4 18.0 1.0 O A:HOH743 2.4 13.8 1.0 O A:HOH788 2.6 30.8 1.0 O A:HOH774 2.8 30.6 1.0 NH2 A:ARG150 3.0 37.9 1.0 CG A:ASP147 3.4 17.4 1.0 OD2 A:ASP147 3.7 18.6 1.0 CZ A:ARG150 4.1 37.0 1.0 NH1 A:ARG150 4.3 38.1 1.0 O A:LEU143 4.5 10.4 1.0 CB A:ASP147 4.8 15.2 1.0

Samarium binding site 3 out of 3 in the Crystal Structure of Nudix Hydrolase DR1025 in Complex with Sm+3


Mono view


Stereo pair view

A full contact list of Samarium with other atoms in the Sm binding site number 3 of Crystal Structure of Nudix Hydrolase DR1025 in Complex with Sm+3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Sm303 b:0.8 occ:1.00 O A:HOH753 2.5 14.8 1.0 OE2 A:GLU12 2.8 18.2 1.0 O A:GLY90 2.9 8.0 1.0 OE1 A:GLU12 3.4 13.4 1.0 CD A:GLU12 3.5 16.9 1.0 C A:GLY90 3.9 6.6 1.0 NH1 A:ARG86 3.9 10.8 1.0 N A:LEU92 4.2 7.2 1.0 CA A:VAL91 4.3 6.4 1.0 CG A:LEU92 4.3 7.4 1.0 N A:VAL91 4.5 5.7 1.0 O A:PRO10 4.5 9.6 1.0 C A:VAL91 4.6 7.0 1.0 CD1 A:LEU92 4.7 8.0 1.0 CB A:LEU92 4.8 7.1 1.0 CA A:GLY90 4.9 8.1 1.0 CG A:GLU12 4.9 11.0 1.0

W.Ranatunga, E.E.Hill, J.L.Mooster, E.L.Holbrook, U.Schulze-Gahmen, W.Xu, M.J.Bessman, S.E.Brenner, S.R.Holbrook. Structural Studies of the Nudix Hydrolase DR1025 From Deinococcus Radiodurans and Its Ligand Complexes. J.Mol.Biol. V. 339 103 2004.
ISSN: ISSN 0022-2836
PubMed: 15123424
DOI: 10.1016/J.JMB.2004.01.065