Fluorine in PDB 2iy7: Crystal Structure of the Sialyltransferase PM0188 with Cmp-3FNEUAC

The structure of Crystal Structure of the Sialyltransferase PM0188 with Cmp-3FNEUAC, PDB code: 2iy7 was solved by D.U.Kim, H.S.Cho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 1.85
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	64.024, 65.346, 106.403, 90.00, 90.00, 90.00
R / Rfree (%)	19.9 / 20.5

The binding sites of Fluorine atom in the Crystal Structure of the Sialyltransferase PM0188 with Cmp-3FNEUAC (pdb code 2iy7). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Crystal Structure of the Sialyltransferase PM0188 with Cmp-3FNEUAC, PDB code: 2iy7:

Fluorine binding site 1 out of 1 in the Crystal Structure of the Sialyltransferase PM0188 with Cmp-3FNEUAC


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 the Sialyltransferase PM0188 with Cmp-3FNEUAC within 5.0Å range: probe atom residue distance (Å) B Occ A:F1414 b:19.1 occ:1.00 F3A A:CSF1414 0.0 19.1 1.0 C3A A:CSF1414 1.4 30.9 1.0 C2A A:CSF1414 2.4 28.8 1.0 C4A A:CSF1414 2.4 33.4 1.0 OD2 A:ASP141 2.7 12.7 1.0 C1A A:CSF1414 2.8 29.3 1.0 O4A A:CSF1414 2.9 38.9 1.0 C5A A:CSF1414 2.9 30.7 1.0 O6A A:CSF1414 3.0 28.3 1.0 OAA A:CSF1414 3.2 30.4 1.0 O A:HOH2100 3.3 27.8 1.0 C6A A:CSF1414 3.3 30.6 1.0 CG A:ASP141 3.4 12.3 1.0 OBA A:CSF1414 3.4 31.8 1.0 O1A A:CSF1414 3.5 27.2 1.0 OD1 A:ASP141 3.6 13.5 1.0 O A:ASP141 4.3 9.2 1.0 N5A A:CSF1414 4.3 26.6 1.0 O7A A:CSF1414 4.5 37.1 1.0 O A:HOH2289 4.5 7.1 1.0 CB A:ALA35 4.5 10.2 1.0 CB A:ASP141 4.6 8.4 1.0 C7A A:CSF1414 4.7 33.5 1.0 C A:ASP141 4.7 8.3 1.0

D.U.Kim, J.H.Yoo, Y.J.Lee, K.S.Kim, H.S.Cho. Structural Analysis of Sialyltransferase PM0188 From Pasteurella Multocida Complexed with Donor Analogue and Acceptor Sugar. Bmb Rep V. 41 48 2008.
ISSN: ISSN 1976-6696
PubMed: 18304450
DOI: 10.5483/BMBREP.2008.41.1.048