Fluorine in PDB 2bh2: Crystal Structure of E. Coli 5-Methyluridine Methyltransferase Ruma in Complex with Ribosomal Rna Substrate and S-Adenosylhomocysteine.

The structure of Crystal Structure of E. Coli 5-Methyluridine Methyltransferase Ruma in Complex with Ribosomal Rna Substrate and S-Adenosylhomocysteine., PDB code: 2bh2 was solved by T.T.Lee, S.Agarwalla, R.M.Stroud, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.15
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	190.061, 63.542, 112.019, 90.00, 125.15, 90.00
R / Rfree (%)	17.4 / 22.9

The structure of Crystal Structure of E. Coli 5-Methyluridine Methyltransferase Ruma in Complex with Ribosomal Rna Substrate and S-Adenosylhomocysteine. also contains other interesting chemical elements:

Iron

(Fe)

8 atoms

The binding sites of Fluorine atom in the Crystal Structure of E. Coli 5-Methyluridine Methyltransferase Ruma in Complex with Ribosomal Rna Substrate and S-Adenosylhomocysteine. (pdb code 2bh2). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Crystal Structure of E. Coli 5-Methyluridine Methyltransferase Ruma in Complex with Ribosomal Rna Substrate and S-Adenosylhomocysteine., PDB code: 2bh2:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Crystal Structure of E. Coli 5-Methyluridine Methyltransferase Ruma in Complex with Ribosomal Rna Substrate and S-Adenosylhomocysteine.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of E. Coli 5-Methyluridine Methyltransferase Ruma in Complex with Ribosomal Rna Substrate and S-Adenosylhomocysteine. within 5.0Å range: probe atom residue distance (Å) B Occ C:F1939 b:43.5 occ:1.00 F C:FMU1939 0.0 43.5 1.0 C5 C:FMU1939 1.3 38.5 1.0 C4 C:FMU1939 2.3 37.5 1.0 C6 C:FMU1939 2.3 40.1 1.0 C5M C:FMU1939 2.3 40.8 1.0 O4 C:FMU1939 2.7 34.1 1.0 SG A:CYS389 2.8 45.8 1.0 CB A:CYS389 3.2 35.5 1.0 N A:CYS389 3.2 34.8 1.0 O A:PRO364 3.2 34.0 1.0 OD1 A:ASP363 3.4 33.2 1.0 N3 C:FMU1939 3.4 35.2 1.0 N1 C:FMU1939 3.5 34.1 1.0 O A:HOH2117 3.5 43.6 1.0 CA A:CYS389 3.8 36.9 1.0 C A:SER388 3.8 34.7 1.0 C2 C:FMU1939 3.9 34.0 1.0 CA A:SER388 4.1 33.9 1.0 OE1 A:GLU424 4.1 52.3 1.0 OE2 A:GLU424 4.3 49.6 1.0 C A:PRO364 4.4 32.2 1.0 CG A:ASP363 4.4 29.5 1.0 CD A:GLU424 4.5 45.7 1.0 O A:VAL387 4.6 32.4 1.0 N A:SER388 4.6 32.0 1.0 O A:SER388 4.7 36.4 1.0 C1' C:FMU1939 4.7 34.6 1.0 O A:ASP363 4.8 29.1 1.0 OD2 A:ASP363 4.8 31.1 1.0 C A:VAL387 4.8 30.4 1.0 C A:ASP363 4.8 29.5 1.0 C A:CYS389 5.0 36.9 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of E. Coli 5-Methyluridine Methyltransferase Ruma in Complex with Ribosomal Rna Substrate and S-Adenosylhomocysteine.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of E. Coli 5-Methyluridine Methyltransferase Ruma in Complex with Ribosomal Rna Substrate and S-Adenosylhomocysteine. within 5.0Å range: probe atom residue distance (Å) B Occ D:F1939 b:38.2 occ:1.00 F D:FMU1939 0.0 38.2 1.0 C5 D:FMU1939 1.4 37.3 1.0 C6 D:FMU1939 2.3 36.7 1.0 C5M D:FMU1939 2.4 38.3 1.0 C4 D:FMU1939 2.5 36.0 1.0 SG B:CYS389 2.8 37.9 1.0 O B:PRO364 2.9 27.4 1.0 O4 D:FMU1939 3.0 35.9 1.0 O B:HOH2115 3.2 41.3 1.0 OD1 B:ASP363 3.2 32.5 1.0 N B:CYS389 3.2 32.5 1.0 CB B:CYS389 3.3 31.6 1.0 N1 D:FMU1939 3.6 31.4 1.0 N3 D:FMU1939 3.6 31.6 1.0 C B:SER388 3.8 32.1 1.0 CA B:CYS389 3.9 33.4 1.0 CA B:SER388 4.0 32.4 1.0 C2 D:FMU1939 4.1 30.4 1.0 C B:PRO364 4.1 28.4 1.0 OE2 B:GLU424 4.3 40.8 1.0 CG B:ASP363 4.3 32.2 1.0 O B:VAL387 4.5 29.5 1.0 N B:SER388 4.5 31.9 1.0 O B:ASP363 4.6 27.4 1.0 C B:ASP363 4.6 28.8 1.0 O B:SER388 4.6 32.2 1.0 OD2 B:ASP363 4.7 35.3 1.0 OE1 B:GLU424 4.7 38.5 1.0 C1' D:FMU1939 4.8 30.5 1.0 C B:VAL387 4.8 30.3 1.0 CA B:ALA365 4.8 30.2 1.0 N B:PRO364 4.9 28.7 1.0 CD B:GLU424 4.9 38.3 1.0 N B:ALA365 4.9 29.6 1.0 C B:ALA365 5.0 32.1 1.0 C B:CYS389 5.0 33.4 1.0

T.T.Lee, S.Agarwalla, R.M.Stroud. A Unique Rna Fold in the Ruma-Rna-Cofactor Ternary Complex Contributes to Substrate Selectivity and Enzymatic Function Cell(Cambridge,Mass.) V. 120 599 2005.
ISSN: ISSN 0092-8674
PubMed: 15766524
DOI: 10.1016/J.CELL.2004.12.037