Fluorine in PDB 1ney: Triosephosphate Isomerase in Complex with Dhap

All present enzymatic activity of Triosephosphate Isomerase in Complex with Dhap:
5.3.1.1;

The structure of Triosephosphate Isomerase in Complex with Dhap, PDB code: 1ney was solved by G.Jogl, S.Rozovsky, A.E.Mcdermott, L.Tong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	73.620, 82.800, 38.214, 90.00, 101.75, 90.00
R / Rfree (%)	12.5 / 15

The binding sites of Fluorine atom in the Triosephosphate Isomerase in Complex with Dhap (pdb code 1ney). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Triosephosphate Isomerase in Complex with Dhap, PDB code: 1ney:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Triosephosphate Isomerase in Complex with Dhap


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Triosephosphate Isomerase in Complex with Dhap within 5.0Å range: probe atom residue distance (Å) B Occ A:F168 b:39.2 occ:1.00 F A:FTR168 0.0 39.2 1.0 CZ3 A:FTR168 1.4 11.0 1.0 CE3 A:FTR168 2.3 10.2 1.0 CH2 A:FTR168 2.4 10.6 1.0 O A:LEU174 2.4 12.6 1.0 HE3 A:FTR168 2.5 12.2 1.0 HH2 A:FTR168 2.6 12.7 1.0 HB3 A:LEU174 3.0 10.4 1.0 C A:LEU174 3.1 8.6 1.0 O A:ALA175 3.2 9.9 1.0 C A:ALA175 3.3 7.8 1.0 O A:HOH5350 3.4 31.9 1.0 O A:HOH5334 3.5 31.6 1.0 CD2 A:FTR168 3.6 7.7 1.0 HB2 A:ALA169 3.6 9.9 1.0 HB2 A:LEU174 3.6 10.4 1.0 CZ2 A:FTR168 3.6 9.2 1.0 CB A:LEU174 3.7 8.7 1.0 HA A:ALA176 3.7 9.5 1.0 O A:HOH5366 3.7 42.0 1.0 N A:ALA176 3.7 8.0 1.0 N A:ALA175 3.7 9.5 1.0 CA A:LEU174 3.9 7.9 1.0 CA A:ALA175 3.9 8.5 1.0 HA A:ALA175 3.9 10.2 1.0 H A:ALA176 4.0 9.6 1.0 CE2 A:FTR168 4.1 7.7 1.0 HA A:LEU174 4.2 9.5 1.0 HA A:ALA169 4.2 7.3 1.0 CA A:ALA176 4.3 7.9 1.0 CB A:ALA169 4.4 6.6 1.0 HZ2 A:FTR168 4.4 11.1 1.0 H A:ALA175 4.4 11.4 1.0 HB3 A:ALA169 4.5 9.9 1.0 CA A:ALA169 4.7 6.1 1.0 HB2 A:ALA176 4.9 15.6 1.0 CG A:FTR168 4.9 7.0 1.0 N A:ALA169 5.0 6.1 1.0

Fluorine binding site 2 out of 2 in the Triosephosphate Isomerase in Complex with Dhap


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Triosephosphate Isomerase in Complex with Dhap within 5.0Å range: probe atom residue distance (Å) B Occ B:F168 b:37.0 occ:1.00 F B:FTR168 0.0 37.0 1.0 CZ3 B:FTR168 1.4 8.6 1.0 CE3 B:FTR168 2.3 7.3 1.0 CH2 B:FTR168 2.4 9.6 1.0 O B:LEU174 2.4 11.3 1.0 HE3 B:FTR168 2.5 8.8 1.0 HH2 B:FTR168 2.6 11.5 1.0 C B:LEU174 3.1 6.5 1.0 HB3 B:LEU174 3.1 9.1 1.0 O B:ALA175 3.2 8.8 1.0 C B:ALA175 3.3 6.9 1.0 O B:HOH6268 3.3 36.2 1.0 O B:HOH6262 3.5 17.6 1.0 CZ2 B:FTR168 3.6 7.3 1.0 CD2 B:FTR168 3.6 6.0 1.0 N B:ALA175 3.7 8.1 1.0 HB2 B:LEU174 3.7 9.1 1.0 N B:ALA176 3.7 6.6 1.0 HB2 B:ALA169 3.7 8.6 1.0 CB B:LEU174 3.7 7.6 1.0 HA B:ALA176 3.8 6.7 1.0 CA B:ALA175 3.8 6.6 1.0 HA B:ALA175 3.9 7.9 1.0 CA B:LEU174 4.0 6.3 1.0 H B:ALA176 4.0 7.9 1.0 CE2 B:FTR168 4.1 5.7 1.0 O B:HOH6171 4.2 41.9 1.0 HA B:LEU174 4.2 7.5 1.0 CA B:ALA176 4.3 5.6 1.0 HA B:ALA169 4.3 5.4 1.0 H B:ALA175 4.3 9.7 1.0 HZ2 B:FTR168 4.4 8.8 1.0 CB B:ALA169 4.5 5.8 1.0 HB3 B:ALA169 4.6 8.6 1.0 HZ1 B:LYS134 4.8 30.2 0.6 CA B:ALA169 4.8 4.5 1.0 HB2 B:ALA176 4.9 10.3 1.0 CG B:FTR168 5.0 5.5 1.0 HZ3 B:LYS134 5.0 30.2 0.6

G.Jogl, S.Rozovsky, A.E.Mcdermott, L.Tong. Optimal Alignment For Enzymatic Proton Transfer: Structure of the Michaelis Complex of Triosephosphate Isomerase at 1.2-A Resolution. Proc.Natl.Acad.Sci.Usa V. 100 50 2003.
ISSN: ISSN 0027-8424
PubMed: 12509510
DOI: 10.1073/PNAS.0233793100