Atomistry » Fluorine » PDB 5lz5-5msa » 5m1i
Atomistry »
  Fluorine »
    PDB 5lz5-5msa »
      5m1i »

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: Sun Dec 13 12:27:41 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy