Praseodymium in PDB 2f1r: Crystal Structure of Molybdopterin-Guanine Biosynthesis Protein B (Mobb)

The structure of Crystal Structure of Molybdopterin-Guanine Biosynthesis Protein B (Mobb), PDB code: 2f1r was solved by L.Damodharan, S.Eswaramoorthy, D.Kumaran, S.Swaminathan, S.K.Burley, New York Sgx Research Center For Structuralgenomics (Nysgxrc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	37.980, 63.930, 66.010, 90.00, 95.30, 90.00
R / Rfree (%)	18.6 / 25.3

The structure of Crystal Structure of Molybdopterin-Guanine Biosynthesis Protein B (Mobb) also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Praseodymium atom in the Crystal Structure of Molybdopterin-Guanine Biosynthesis Protein B (Mobb) (pdb code 2f1r). This binding sites where shown within 5.0 Angstroms radius around Praseodymium atom.
In total only one binding site of Praseodymium was determined in the Crystal Structure of Molybdopterin-Guanine Biosynthesis Protein B (Mobb), PDB code: 2f1r:

Praseodymium binding site 1 out of 1 in the Crystal Structure of Molybdopterin-Guanine Biosynthesis Protein B (Mobb)


Mono view


Stereo pair view

A full contact list of Praseodymium with other atoms in the Pr binding site number 1 of Crystal Structure of Molybdopterin-Guanine Biosynthesis Protein B (Mobb) within 5.0Å range: probe atom residue distance (Å) B Occ B:Pr174 b:13.6 occ:1.00 O B:HOH177 3.0 14.3 1.0 O B:HOH183 3.0 12.7 1.0 O B:HOH184 3.0 14.3 1.0 O B:HOH179 3.0 13.4 1.0 O B:HOH176 3.0 13.7 1.0 O B:HOH180 3.0 15.2 1.0 O B:HOH182 3.0 12.1 1.0 O B:HOH175 3.0 17.3 1.0 O B:HOH178 3.0 17.9 1.0 O B:HOH181 3.1 17.0 1.0 O B:TRP143 4.3 10.9 1.0 OE2 B:GLU148 4.6 17.7 1.0 OE1 B:GLU148 4.7 12.3 1.0 O B:HOH241 4.7 24.3 1.0

L.Damodharan, S.Eswaramoorthy, D.Kumaran, S.Swaminathan. Crystal Structure of Molybdopterin-Guanine Dinucleotide Biosynthesis Protein B (Mobb) To Be Published.