Atomistry » Fluorine » PDB 1mmd-1o5f » 1nf0
Atomistry »
  Fluorine »
    PDB 1mmd-1o5f »
      1nf0 »

Fluorine in PDB 1nf0: Triosephosphate Isomerase in Complex with Dhap

Enzymatic activity of Triosephosphate Isomerase in Complex with Dhap

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

Protein crystallography data

The structure of Triosephosphate Isomerase in Complex with Dhap, PDB code: 1nf0 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) 40.00 / 1.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.258, 62.170, 160.684, 90.00, 90.00, 90.00
R / Rfree (%) 21.2 / 26.8

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Triosephosphate Isomerase in Complex with Dhap (pdb code 1nf0). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Triosephosphate Isomerase in Complex with Dhap, PDB code: 1nf0:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in 1nf0

Go back to Fluorine Binding Sites List in 1nf0
Fluorine binding site 1 out of 3 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:0.9
occ:0.57
F A:FTR168 0.0 0.9 0.6
CZ3 A:FTR168 1.3 13.1 0.6
CE3 A:FTR168 2.3 14.7 0.6
CH2 A:FTR168 2.4 23.8 0.6
CH2 A:FTR168 2.7 31.9 0.4
O A:ALA175 3.0 19.4 0.6
C A:ALA175 3.0 17.0 0.6
CZ2 A:FTR168 3.0 20.6 0.4
CZ3 A:FTR168 3.1 32.8 0.4
N A:ALA176 3.2 16.6 0.6
CB A:LEU174 3.3 17.0 0.6
CB A:ALA169 3.5 18.7 0.6
N A:ALA175 3.5 25.4 0.6
C A:LEU174 3.6 23.8 0.6
CA A:ALA176 3.6 19.5 0.6
CD2 A:FTR168 3.6 13.3 0.6
CZ2 A:FTR168 3.6 28.3 0.6
CE2 A:FTR168 3.7 19.7 0.4
CA A:ALA175 3.7 18.2 0.6
F A:FTR168 3.7 25.4 0.4
CA A:ALA176 3.8 20.0 0.4
CE3 A:FTR168 3.8 28.4 0.4
CB A:ALA176 4.0 21.0 0.6
O A:LEU174 4.0 22.5 0.6
N A:ALA176 4.0 19.3 0.4
CB A:ALA176 4.0 27.9 0.4
CD2 A:FTR168 4.1 20.8 0.4
CA A:LEU174 4.1 18.5 0.6
CE2 A:FTR168 4.1 19.9 0.6
O A:ALA175 4.1 16.1 0.4
CD1 A:LEU174 4.2 12.1 0.6
CA A:ALA169 4.2 17.6 0.6
C A:ALA175 4.2 16.5 0.4
CG A:LEU174 4.3 27.7 0.6
O A:LEU174 4.5 31.2 0.4
N A:ALA169 4.5 11.6 0.6
NE1 A:FTR168 4.7 11.2 0.4
O A:FTR168 4.8 19.4 0.4
CG A:FTR168 4.9 12.8 0.6
C A:FTR168 5.0 16.9 0.6

Fluorine binding site 2 out of 3 in 1nf0

Go back to Fluorine Binding Sites List in 1nf0
Fluorine binding site 2 out of 3 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
A:F168

b:25.4
occ:0.43
F A:FTR168 0.0 25.4 0.4
CG A:LEU174 1.1 27.7 0.6
CB A:LEU174 1.1 17.0 0.6
CZ3 A:FTR168 1.3 32.8 0.4
CD1 A:LEU174 1.6 12.1 0.6
CE3 A:FTR168 2.3 28.4 0.4
CH2 A:FTR168 2.4 31.9 0.4
CD2 A:LEU174 2.5 20.8 0.6
CA A:LEU174 2.6 18.5 0.6
N A:LEU174 3.2 13.5 0.6
OG1 A:THR172 3.5 13.3 0.6
CD2 A:FTR168 3.6 20.8 0.4
O A:FTR168 3.6 16.0 0.6
C A:LEU174 3.6 23.8 0.6
CZ2 A:FTR168 3.7 20.6 0.4
F A:FTR168 3.7 0.9 0.6
CE3 A:FTR168 3.9 14.7 0.6
CE2 A:FTR168 4.1 19.7 0.4
C A:GLY173 4.1 16.7 0.6
CZ3 A:FTR168 4.3 13.1 0.6
O A:LEU174 4.3 22.5 0.6
N A:ALA175 4.3 25.4 0.6
O A:GLY173 4.5 34.6 0.6
C A:FTR168 4.5 16.9 0.6
CD1 A:LEU131 4.5 15.6 1.0
CB A:THR172 4.6 17.6 0.6
CA A:ALA169 4.6 17.6 0.6
O A:FTR168 4.8 19.4 0.4
N A:ALA169 4.9 11.6 0.6
CG A:FTR168 4.9 9.3 0.4
O A:THR172 4.9 6.5 0.6

Fluorine binding site 3 out of 3 in 1nf0

Go back to Fluorine Binding Sites List in 1nf0
Fluorine binding site 3 out of 3 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 3 of Triosephosphate Isomerase in Complex with Dhap within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F168

b:35.3
occ:1.00
F B:FTR168 0.0 35.3 1.0
CZ3 B:FTR168 1.3 27.9 1.0
CE3 B:FTR168 2.3 21.1 1.0
CH2 B:FTR168 2.4 27.1 1.0
O B:HOH1348 2.8 56.8 1.0
O B:HOH1332 2.8 84.9 1.0
O B:LEU174 3.3 25.2 1.0
O B:ALA175 3.6 26.3 1.0
CD2 B:FTR168 3.6 16.0 1.0
CZ2 B:FTR168 3.7 24.3 1.0
O B:HOH1269 3.7 20.5 1.0
C B:ALA175 3.8 21.3 1.0
N B:ALA176 3.9 15.7 1.0
CE2 B:FTR168 4.1 13.0 1.0
CA B:ALA176 4.2 24.9 1.0
C B:LEU174 4.2 19.7 1.0
CB B:ALA169 4.4 18.2 1.0
CA B:ALA175 4.6 13.1 1.0
CB B:LEU174 4.6 26.2 1.0
CA B:ALA169 4.7 13.2 1.0
O B:FTR168 4.8 14.6 1.0
N B:ALA175 4.9 15.3 1.0
CG B:FTR168 4.9 15.4 1.0

Reference:

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
Page generated: Wed Jul 31 12:07:23 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy