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Fluorine in PDB 1ss9: Crystal Structural Analysis of Active Site Mutant Q189E of Lgtc

Enzymatic activity of Crystal Structural Analysis of Active Site Mutant Q189E of Lgtc

All present enzymatic activity of Crystal Structural Analysis of Active Site Mutant Q189E of Lgtc:
2.4.1.44;

Protein crystallography data

The structure of Crystal Structural Analysis of Active Site Mutant Q189E of Lgtc, PDB code: 1ss9 was solved by L.L.Lairson, C.P.Chiu, H.D.Ly, S.He, W.W.Wakarchuk, N.C.Strynadka, S.G.Withers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.30 / 2.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 39.850, 75.934, 86.905, 90.00, 90.00, 90.00
R / Rfree (%) 21.7 / 28.3

Other elements in 1ss9:

The structure of Crystal Structural Analysis of Active Site Mutant Q189E of Lgtc also contains other interesting chemical elements:

Manganese (Mn) 1 atom

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structural Analysis of Active Site Mutant Q189E of Lgtc (pdb code 1ss9). 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 Structural Analysis of Active Site Mutant Q189E of Lgtc, PDB code: 1ss9:

Fluorine binding site 1 out of 1 in 1ss9

Go back to Fluorine Binding Sites List in 1ss9
Fluorine binding site 1 out of 1 in the Crystal Structural Analysis of Active Site Mutant Q189E of Lgtc


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structural Analysis of Active Site Mutant Q189E of Lgtc within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F401

b:36.4
occ:1.00
F2' A:UPF401 0.0 36.4 1.0
C2' A:UPF401 1.4 37.5 1.0
C1' A:UPF401 2.4 35.6 1.0
C3' A:UPF401 2.5 39.8 1.0
O3B A:UPF401 2.8 27.9 1.0
ND2 A:ASN153 2.8 0.6 1.0
O3' A:UPF401 2.9 38.1 1.0
O1B A:UPF401 2.9 20.6 1.0
SG A:CYS246 3.2 36.3 1.0
CE1 A:HIS244 3.5 5.5 1.0
PB A:UPF401 3.5 19.0 1.0
CG A:ASN153 3.7 0.6 1.0
O5' A:UPF401 3.7 37.9 1.0
OE1 A:GLU189 3.7 24.7 1.0
OD1 A:ASN153 3.8 0.7 1.0
C4' A:UPF401 3.8 39.2 1.0
CB A:CYS246 4.0 19.5 1.0
NE2 A:HIS244 4.2 6.5 1.0
C5' A:UPF401 4.2 39.3 1.0
MN A:MN400 4.2 7.1 1.0
O4' A:UPF401 4.3 41.7 1.0
ND1 A:HIS244 4.3 8.2 1.0
O2B A:UPF401 4.5 19.6 1.0
CA A:CYS246 4.5 18.7 1.0
O3A A:UPF401 4.6 20.5 1.0
OD1 A:ASP103 4.6 16.7 1.0
CD A:GLU189 4.7 27.2 1.0
OD2 A:ASP130 4.9 16.2 1.0
OE2 A:GLU189 4.9 28.9 1.0
SD A:MET210 5.0 12.7 1.0

Reference:

L.L.Lairson, C.P.Chiu, H.D.Ly, S.He, W.W.Wakarchuk, N.C.Strynadka, S.G.Withers. Intermediate Trapping on A Mutant Retaining Alpha-Galactosyltransferase Identifies An Unexpected Aspartate Residue. J.Biol.Chem. V. 279 28339 2004.
ISSN: ISSN 0021-9258
PubMed: 15075344
DOI: 10.1074/JBC.M400451200
Page generated: Wed Jul 31 12:51:44 2024

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