Mercury in PDB 4nho: Structure of the Spliceosomal Dead-Box Protein PRP28

All present enzymatic activity of Structure of the Spliceosomal Dead-Box Protein PRP28:
3.6.4.13;

The structure of Structure of the Spliceosomal Dead-Box Protein PRP28, PDB code: 4nho was solved by S.Moehlmann, P.Neumann, R.Ficner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.82 / 2.00
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	125.430, 136.770, 73.220, 90.00, 90.00, 90.00
R / Rfree (%)	19.3 / 21.8

The binding sites of Mercury atom in the Structure of the Spliceosomal Dead-Box Protein PRP28 (pdb code 4nho). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 2 binding sites of Mercury where determined in the Structure of the Spliceosomal Dead-Box Protein PRP28, PDB code: 4nho:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in the Structure of the Spliceosomal Dead-Box Protein PRP28


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Structure of the Spliceosomal Dead-Box Protein PRP28 within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg909 b:48.4 occ:0.47 HG A:HG909 0.0 48.4 0.5 CD2 A:LEU540 2.6 32.7 1.0 SG A:CYS543 2.6 55.2 1.0 HG A:HG909 2.8 60.0 0.3 SD A:MET570 3.1 54.5 1.0 CG1 A:ILE472 3.2 53.6 1.0 CB A:ILE472 3.2 47.9 1.0 CG2 A:VAL546 3.4 47.8 1.0 O A:TYR545 3.7 40.9 1.0 CB A:CYS543 3.7 51.4 1.0 N A:ILE472 3.8 45.9 1.0 CG A:LEU540 3.9 0.9 1.0 CD1 A:LEU540 4.0 91.9 1.0 CE A:MET570 4.0 40.8 1.0 CA A:ILE472 4.1 44.2 1.0 CA A:VAL546 4.3 43.6 1.0 CB A:VAL546 4.4 47.4 1.0 CG2 A:ILE472 4.4 51.7 1.0 CD1 A:ILE472 4.4 53.9 1.0 C A:TYR545 4.5 40.3 1.0 CG A:MET570 4.5 46.2 1.0 O A:ILE472 4.6 38.2 1.0 CG1 A:VAL546 4.8 49.2 1.0 C A:ALA471 4.8 50.6 1.0 N A:VAL546 4.8 37.6 1.0 C A:ILE472 4.9 40.2 1.0

Mercury binding site 2 out of 2 in the Structure of the Spliceosomal Dead-Box Protein PRP28


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Structure of the Spliceosomal Dead-Box Protein PRP28 within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg909 b:60.0 occ:0.33 HG A:HG909 0.0 60.0 0.3 SG A:CYS543 2.5 55.2 1.0 CE A:MET570 2.5 40.8 1.0 CG2 A:VAL546 2.7 47.8 1.0 HG A:HG909 2.8 48.4 0.5 CB A:CYS543 3.0 51.4 1.0 SD A:MET570 3.1 54.5 1.0 O A:TYR545 3.4 40.9 1.0 C A:CYS543 3.5 51.5 1.0 N A:TYR545 3.6 37.6 1.0 O A:CYS543 3.6 55.4 1.0 C A:TYR545 3.7 40.3 1.0 N A:THR544 3.8 45.4 1.0 CA A:CYS543 3.8 51.8 1.0 CD2 A:LEU540 4.0 32.7 1.0 CB A:VAL546 4.1 47.4 1.0 N A:VAL546 4.1 37.6 1.0 C A:THR544 4.2 41.8 1.0 CA A:TYR545 4.3 37.7 1.0 CA A:VAL546 4.3 43.6 1.0 CA A:THR544 4.3 44.0 1.0 CG A:MET570 4.5 46.2 1.0 CD A:ARG600 5.0 46.5 1.0

S.Mohlmann, R.Mathew, P.Neumann, A.Schmitt, R.Luhrmann, R.Ficner. Structural and Functional Analysis of the Human Spliceosomal Dead-Box Helicase PRP28. Acta Crystallogr.,Sect.D V. 70 1622 2014.
ISSN: ISSN 0907-4449
PubMed: 24914973
DOI: 10.1107/S1399004714006439