Yttrium in PDB 3uf3: Crystal Structure of Multidrug Resistant Hiv-1 Protease Clinical Isolate PR20

The structure of Crystal Structure of Multidrug Resistant Hiv-1 Protease Clinical Isolate PR20, PDB code: 3uf3 was solved by J.Agniswamy, S.Chen-Hsiang, A.Aniana, J.M.Sayer, J.M.Louis, I.T.Weber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.63
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	44.343, 45.848, 103.987, 90.00, 90.00, 90.00
R / Rfree (%)	18.8 / 22.2

The binding sites of Yttrium atom in the Crystal Structure of Multidrug Resistant Hiv-1 Protease Clinical Isolate PR20 (pdb code 3uf3). This binding sites where shown within 5.0 Angstroms radius around Yttrium atom.
In total 2 binding sites of Yttrium where determined in the Crystal Structure of Multidrug Resistant Hiv-1 Protease Clinical Isolate PR20, PDB code: 3uf3:
Jump to Yttrium binding site number: 1; 2;

Yttrium binding site 1 out of 2 in the Crystal Structure of Multidrug Resistant Hiv-1 Protease Clinical Isolate PR20


Mono view


Stereo pair view

A full contact list of Yttrium with other atoms in the Y binding site number 1 of Crystal Structure of Multidrug Resistant Hiv-1 Protease Clinical Isolate PR20 within 5.0Å range: probe atom residue distance (Å) B Occ A:Y201 b:37.2 occ:0.60 O A:HOH458 1.5 18.5 0.5 O A:HOH440 1.7 20.7 0.5 OE2 A:GLU34 2.2 30.7 0.5 OE2 A:GLU34 2.5 25.8 0.5 OE1 A:GLU34 2.5 28.9 0.5 OE1 A:GLU34 2.6 28.1 0.5 CD A:GLU34 2.7 28.6 0.5 O A:HOH439 2.7 23.6 0.5 CD A:GLU34 2.9 29.1 0.5 O A:HOH441 3.3 35.2 0.5 O A:HOH442 3.7 36.3 0.5 CG A:GLU34 4.2 26.8 0.5 CG A:GLU34 4.4 25.5 0.5 O A:THR80 4.6 29.6 1.0 OD2 A:ASP35 4.9 32.3 0.5

Yttrium binding site 2 out of 2 in the Crystal Structure of Multidrug Resistant Hiv-1 Protease Clinical Isolate PR20


Mono view


Stereo pair view

A full contact list of Yttrium with other atoms in the Y binding site number 2 of Crystal Structure of Multidrug Resistant Hiv-1 Protease Clinical Isolate PR20 within 5.0Å range: probe atom residue distance (Å) B Occ B:Y202 b:39.8 occ:0.70 O A:HOH437 1.9 36.2 1.0 O B:HOH436 2.4 23.1 0.9 O B:HOH438 2.4 29.6 0.6 OD2 B:ASP25 4.1 25.5 1.0 O B:HOH450 4.2 37.5 0.7 OD2 A:ASP25 4.3 25.4 1.0 O A:HOH417 4.4 40.8 1.0 OD1 B:ASP25 4.7 24.5 1.0 OD1 A:ASP25 4.7 21.9 1.0 CG B:ASP25 4.8 21.1 1.0 O B:GLY27 4.9 20.9 1.0 O A:GLY27 5.0 22.5 1.0

J.Agniswamy, C.H.Shen, A.Aniana, J.M.Sayer, J.M.Louis, I.T.Weber. Hiv-1 Protease with 20 Mutations Exhibits Extreme Resistance to Clinical Inhibitors Through Coordinated Structural Rearrangements. Biochemistry V. 51 2819 2012.
ISSN: ISSN 0006-2960
PubMed: 22404139
DOI: 10.1021/BI2018317