Samarium in PDB 2o3h: Crystal Structure of the Human C65A Ape

All present enzymatic activity of Crystal Structure of the Human C65A Ape:
4.2.99.18;

The structure of Crystal Structure of the Human C65A Ape, PDB code: 2o3h was solved by M.M.Georgiadis, R.K.Gaur, S.Delaplane, J.Svenson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.90
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	46.693, 143.604, 45.385, 90.00, 90.00, 90.00
R / Rfree (%)	17.7 / 22.6

The binding sites of Samarium atom in the Crystal Structure of the Human C65A Ape (pdb code 2o3h). 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 the Human C65A Ape, PDB code: 2o3h:
Jump to Samarium binding site number: 1; 2; 3;

Samarium binding site 1 out of 3 in the Crystal Structure of the Human C65A Ape


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 the Human C65A Ape within 5.0Å range: probe atom residue distance (Å) B Occ A:Sm400 b:16.2 occ:1.00 O A:HOH646 2.4 22.2 1.0 OE2 A:GLU217 2.4 16.3 1.0 O A:HOH506 2.5 26.6 1.0 OE1 A:GLU216 2.5 13.1 1.0 OE1 A:GLU217 2.5 17.1 1.0 OE2 A:GLU216 2.6 21.9 1.0 CD A:GLU217 2.8 13.5 1.0 CD A:GLU216 2.9 15.2 1.0 NH2 A:ARG237 4.2 13.4 1.0 O A:HOH630 4.2 41.2 1.0 CG A:GLU217 4.3 10.7 1.0 CG A:GLU216 4.3 16.1 1.0 O A:HOH508 4.5 12.4 1.0 O A:HOH711 4.6 28.1 1.0 O A:HOH726 4.8 32.1 1.0 N A:GLU217 4.9 10.1 1.0 CB A:GLU216 5.0 11.7 1.0

Samarium binding site 2 out of 3 in the Crystal Structure of the Human C65A Ape


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 the Human C65A Ape within 5.0Å range: probe atom residue distance (Å) B Occ A:Sm401 b:12.6 occ:0.80 SM A:SM401 0.0 12.6 0.8 SM A:SM401 1.5 10.9 0.2 O A:HOH789 2.0 32.8 1.0 OE2 A:GLU96 2.1 20.1 1.0 O A:HOH703 2.1 36.2 1.0 OD1 A:ASP70 2.3 17.7 1.0 O A:HOH676 2.4 12.6 1.0 O A:HOH593 2.5 21.2 1.0 CD A:GLU96 2.8 16.6 1.0 OE1 A:GLU96 2.8 25.0 1.0 CG A:ASP70 3.4 15.5 1.0 CB A:ASP70 4.2 12.1 1.0 CG A:GLU96 4.2 16.2 1.0 NZ A:LYS98 4.3 23.6 1.0 OD2 A:ASP70 4.3 17.5 1.0 O A:HOH559 4.3 24.7 1.0 OD2 A:ASP308 4.4 12.1 1.0 CE A:LYS98 4.5 23.2 1.0 CA A:ASP70 4.5 12.4 1.0 O A:HOH725 4.6 35.9 1.0 OD1 A:ASP308 4.7 12.7 1.0 ND2 A:ASN68 4.8 7.6 1.0 OH A:TYR171 4.8 17.2 1.0 O A:HOH709 4.9 28.9 1.0 OXT A:ACT503 4.9 34.6 1.0 CG A:ASP308 5.0 12.8 1.0

Samarium binding site 3 out of 3 in the Crystal Structure of the Human C65A Ape


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 the Human C65A Ape within 5.0Å range: probe atom residue distance (Å) B Occ A:Sm401 b:10.9 occ:0.20 SM A:SM401 0.0 10.9 0.2 SM A:SM401 1.5 12.6 0.8 O A:HOH703 2.0 36.2 1.0 O A:HOH676 2.5 12.6 1.0 OE1 A:GLU96 2.5 25.0 1.0 O A:HOH789 2.7 32.8 1.0 O A:HOH559 2.9 24.7 1.0 OE2 A:GLU96 3.0 20.1 1.0 CD A:GLU96 3.1 16.6 1.0 O A:HOH593 3.7 21.2 1.0 OD1 A:ASP70 3.8 17.7 1.0 O A:HOH709 3.9 28.9 1.0 OH A:TYR171 4.0 17.2 1.0 O A:HOH569 4.1 16.6 1.0 O A:HOH516 4.5 16.4 1.0 OD1 A:ASN68 4.5 14.4 1.0 OD2 A:ASP308 4.6 12.1 1.0 CG A:GLU96 4.6 16.2 1.0 NE2 A:HIS309 4.7 9.5 1.0 CG A:ASP70 4.7 15.5 1.0 OXT A:ACT503 4.8 34.6 1.0 ND2 A:ASN68 4.8 7.6 1.0 OD1 A:ASP308 4.9 12.7 1.0

M.M.Georgiadis, M.Luo, R.K.Gaur, S.Delaplane, X.Li, M.R.Kelley. Evolution of the Redox Function in Mammalian Apurinic/Apyrimidinic Endonuclease Mutat.Res. V. 643 54 2008.
ISSN: ISSN 0027-5107
PubMed: 18579163
DOI: 10.1016/J.MRFMMM.2008.04.008