Fluorine in PDB 8udi: Crystal Structure of Helicobacter Pylori Glutamate Racemase Bound to D-Glutamate and A Crystallographic Artifact

Protein crystallography data

The structure of Crystal Structure of Helicobacter Pylori Glutamate Racemase Bound to D-Glutamate and A Crystallographic Artifact, PDB code: 8udi was solved by J.Propp, M.A.Spies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 66.54 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 62.317, 81.969, 113.937, 90, 90, 90
R / Rfree (%) 19 / 23.1

Other elements in 8udi:

The structure of Crystal Structure of Helicobacter Pylori Glutamate Racemase Bound to D-Glutamate and A Crystallographic Artifact also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of Helicobacter Pylori Glutamate Racemase Bound to D-Glutamate and A Crystallographic Artifact (pdb code 8udi). 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 Helicobacter Pylori Glutamate Racemase Bound to D-Glutamate and A Crystallographic Artifact, PDB code: 8udi:

Fluorine binding site 1 out of 1 in 8udi

Go back to Fluorine Binding Sites List in 8udi
Fluorine binding site 1 out of 1 in the Crystal Structure of Helicobacter Pylori Glutamate Racemase Bound to D-Glutamate and A Crystallographic Artifact


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 Helicobacter Pylori Glutamate Racemase Bound to D-Glutamate and A Crystallographic Artifact within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F302

b:62.9
occ:0.86
F01 A:WAW302 0.0 62.9 0.9
C02 A:WAW302 1.4 63.4 0.9
H051 A:WAW302 2.3 73.8 0.9
N30 A:WAW302 2.3 63.0 0.9
C03 A:WAW302 2.4 63.7 0.9
OE2 A:GLU246 2.7 61.0 1.0
N04 A:WAW302 2.9 60.8 0.9
C05 A:WAW302 3.0 61.5 0.9
CD A:GLU246 3.2 63.7 1.0
H192 A:WAW302 3.4 68.3 0.9
CB A:GLU246 3.5 57.6 1.0
C29 A:WAW302 3.5 65.1 0.9
N27 A:WAW302 3.6 66.5 0.9
CG A:GLU246 3.7 57.3 1.0
C19 A:WAW302 3.8 57.0 0.9
O09 A:WAW302 3.8 59.7 0.9
OE1 A:GLU246 3.9 66.8 1.0
C28 A:WAW302 4.0 66.7 0.9
C06 A:WAW302 4.2 58.9 0.9
C08 A:WAW302 4.2 61.9 0.9
C26 A:WAW302 4.3 58.1 0.9
H191 A:WAW302 4.4 68.3 0.9
H291 A:WAW302 4.4 78.1 0.9
CD2 A:PHE236 4.5 50.8 1.0
N07 A:WAW302 4.5 62.6 0.9
CA A:GLU246 4.5 50.6 1.0
H062 A:WAW302 4.5 70.7 0.9
H261 A:WAW302 4.6 69.7 0.9
CE2 A:PHE236 4.7 54.8 1.0
O A:GLU246 4.8 53.2 1.0
C A:GLU246 4.9 53.1 1.0
H151 A:WAW302 4.9 80.3 0.9
H262 A:WAW302 5.0 69.7 0.9
C20 A:WAW302 5.0 55.6 0.9

Reference:

J.Propp, M.A.Spies. Structure of H. Pylori Glutamate Racemace with A Crystallographic Artifact To Be Published.
Page generated: Thu Oct 31 19:59:17 2024

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