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Fluorine in PDB 4f60: Crystal Structure of Rhodococcus Rhodochrous Haloalkane Dehalogenase Mutant (T148L, G171Q, A172V, C176F).

Enzymatic activity of Crystal Structure of Rhodococcus Rhodochrous Haloalkane Dehalogenase Mutant (T148L, G171Q, A172V, C176F).

All present enzymatic activity of Crystal Structure of Rhodococcus Rhodochrous Haloalkane Dehalogenase Mutant (T148L, G171Q, A172V, C176F).:
3.8.1.5;

Protein crystallography data

The structure of Crystal Structure of Rhodococcus Rhodochrous Haloalkane Dehalogenase Mutant (T148L, G171Q, A172V, C176F)., PDB code: 4f60 was solved by M.Plevaka, I.Kuta-Smatanova, P.Rezacova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.02 / 1.45
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 52.018, 69.930, 85.352, 90.00, 90.00, 90.00
R / Rfree (%) 15 / 17.1

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of Rhodococcus Rhodochrous Haloalkane Dehalogenase Mutant (T148L, G171Q, A172V, C176F). (pdb code 4f60). 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 Rhodococcus Rhodochrous Haloalkane Dehalogenase Mutant (T148L, G171Q, A172V, C176F)., PDB code: 4f60:

Fluorine binding site 1 out of 1 in 4f60

Go back to Fluorine Binding Sites List in 4f60
Fluorine binding site 1 out of 1 in the Crystal Structure of Rhodococcus Rhodochrous Haloalkane Dehalogenase Mutant (T148L, G171Q, A172V, C176F).


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 Rhodococcus Rhodochrous Haloalkane Dehalogenase Mutant (T148L, G171Q, A172V, C176F). within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F301

b:15.1
occ:1.00
 O A:HOH685 3.0 35.9 1.0
NE1 A:TRP107 3.3 19.3 1.0
N A:PRO206 3.4 19.9 1.0
ND2 A:ASN41 3.4 18.8 1.0
CA A:PRO206 3.5 19.9 1.0
CD A:PRO206 3.6 20.6 1.0
CZ A:PHE168 3.7 18.9 1.0
C A:PHE205 3.7 19.5 1.0
CD1 A:TRP107 3.8 18.9 1.0
CB A:PHE205 3.8 19.5 1.0
CB A:PRO206 3.8 20.6 1.0
CD1 A:LEU209 3.9 21.9 1.0
O A:PHE205 4.0 20.3 1.0
CE1 A:PHE168 4.0 19.9 1.0
CB A:ASN41 4.1 18.1 1.0
CG A:LEU209 4.2 21.4 1.0
CG A:ASN41 4.2 19.2 1.0
CG A:PRO206 4.3 20.6 1.0
CD2 A:LEU209 4.4 22.4 1.0
CA A:PHE205 4.4 19.5 1.0
CE2 A:PHE149 4.5 20.0 1.0
CE2 A:TRP107 4.5 18.4 1.0
CE2 A:PHE168 4.6 17.2 1.0
CG A:PHE205 4.9 18.9 1.0
OD2 A:ASP106 4.9 17.8 1.0
OD1 A:ASP106 4.9 26.6 1.0
C A:PRO206 4.9 20.9 1.0
O A:HOH440 4.9 29.0 1.0

Reference:

T.Koudelakova, R.Chaloupkova, J.Brezovsky, Z.Prokop, E.Sebestova, M.Hesseler, M.Khabiri, M.Plevaka, D.Kulik, I.Kuta Smatanova, P.Rezacova, R.Ettrich, U.T.Bornscheuer, J.Damborsky. Engineering Enzyme Stability and Resistance to An Organic Cosolvent By Modification of Residues in the Access Tunnel. Angew.Chem.Int.Ed.Engl. V. 52 1959 2013.
ISSN: ISSN 1433-7851
PubMed: 23303607
DOI: 10.1002/ANIE.201206708
Page generated: Sun Dec 13 12:02:20 2020

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