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Fluorine in PDB 5m1i: Structure of GH36 Alpha-Galactosidase From Thermotoga Maritima in A Covalent Complex with A Cyclopropyl Carbasugar.

Enzymatic activity of Structure of GH36 Alpha-Galactosidase From Thermotoga Maritima in A Covalent Complex with A Cyclopropyl Carbasugar.

All present enzymatic activity of Structure of GH36 Alpha-Galactosidase From Thermotoga Maritima in A Covalent Complex with A Cyclopropyl Carbasugar.:
3.2.1.22;

Protein crystallography data

The structure of Structure of GH36 Alpha-Galactosidase From Thermotoga Maritima in A Covalent Complex with A Cyclopropyl Carbasugar., PDB code: 5m1i was solved by R.Pengelly, T.Gloster, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 68.52 / 1.55
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 66.903, 96.239, 97.589, 90.00, 90.00, 90.00
R / Rfree (%) 15.4 / 18.3

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Structure of GH36 Alpha-Galactosidase From Thermotoga Maritima in A Covalent Complex with A Cyclopropyl Carbasugar. (pdb code 5m1i). 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 Structure of GH36 Alpha-Galactosidase From Thermotoga Maritima in A Covalent Complex with A Cyclopropyl Carbasugar., PDB code: 5m1i:

Fluorine binding site 1 out of 1 in 5m1i

Go back to Fluorine Binding Sites List in 5m1i
Fluorine binding site 1 out of 1 in the Structure of GH36 Alpha-Galactosidase From Thermotoga Maritima in A Covalent Complex with A Cyclopropyl Carbasugar.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structure of GH36 Alpha-Galactosidase From Thermotoga Maritima in A Covalent Complex with A Cyclopropyl Carbasugar. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F607

b:20.7
occ:1.00
 FAF A:7D8607 0.0 20.7 1.0
CAC A:7D8607 1.4 16.4 1.0
CAB A:7D8607 2.4 16.5 1.0
CAD A:7D8607 2.4 16.8 1.0
SG A:CYS368 2.9 12.8 0.5
OAK A:7D8607 2.9 16.4 1.0
OD1 A:ASP387 2.9 17.3 1.0
NH1 A:ARG383 3.3 16.4 1.0
NE1 A:TRP65 3.3 19.0 1.0
OD2 A:ASP327 3.4 17.9 1.0
OD1 A:ASP327 3.5 17.0 1.0
CAG A:7D8607 3.6 16.8 1.0
CZ2 A:TRP65 3.7 17.8 1.0
CAA A:7D8607 3.7 16.5 1.0
CG A:ASP327 3.8 17.1 1.0
CG A:ASP387 3.8 17.6 1.0
CE2 A:TRP65 3.8 17.3 1.0
NH2 A:ARG383 3.9 15.1 1.0
OD2 A:ASP387 3.9 17.3 1.0
CAI A:7D8607 4.0 15.9 1.0
CZ A:ARG383 4.0 15.0 1.0
OAJ A:7D8607 4.1 15.5 1.0
CAH A:7D8607 4.2 15.6 1.0
CB A:CYS368 4.3 21.8 0.5
SG A:CYS368 4.5 30.5 0.5
CD1 A:TRP65 4.5 17.4 1.0
CB A:CYS368 4.5 13.4 0.5
OH A:TYR191 4.6 17.2 1.0
CE A:LYS325 4.8 16.1 1.0
CH2 A:TRP65 4.9 17.0 1.0
NZ A:LYS325 5.0 15.4 1.0

Reference:

C.Adamson, R.J.Pengelly, S.Shamsi Kazem Abadi, S.Chakladar, J.Draper, R.Britton, T.M.Gloster, A.J.Bennet. Structural Snapshots For Mechanism-Based Inactivation of A Glycoside Hydrolase By Cyclopropyl Carbasugars. Angew.Chem.Int.Ed.Engl. V. 55 14978 2016.
ISSN: ESSN 1521-3773
PubMed: 27783466
DOI: 10.1002/ANIE.201607431
Page generated: Tue Jul 15 05:10:40 2025

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