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Fluorine in PDB 4dpt: Crystal Structure of Staphylococcus Epidermidis Mevalonate Diphosphate Decarboxylase Complexed with Inhibitor 6-Fmvapp and Atpgs

Enzymatic activity of Crystal Structure of Staphylococcus Epidermidis Mevalonate Diphosphate Decarboxylase Complexed with Inhibitor 6-Fmvapp and Atpgs

All present enzymatic activity of Crystal Structure of Staphylococcus Epidermidis Mevalonate Diphosphate Decarboxylase Complexed with Inhibitor 6-Fmvapp and Atpgs:
4.1.1.33;

Protein crystallography data

The structure of Crystal Structure of Staphylococcus Epidermidis Mevalonate Diphosphate Decarboxylase Complexed with Inhibitor 6-Fmvapp and Atpgs, PDB code: 4dpt was solved by M.L.Barta, W.J.Mcwhorter, B.V.Geisbrecht, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.48 / 2.19
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 102.251, 82.460, 93.649, 90.00, 122.34, 90.00
R / Rfree (%) 18.6 / 24.1

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of Staphylococcus Epidermidis Mevalonate Diphosphate Decarboxylase Complexed with Inhibitor 6-Fmvapp and Atpgs (pdb code 4dpt). 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 Staphylococcus Epidermidis Mevalonate Diphosphate Decarboxylase Complexed with Inhibitor 6-Fmvapp and Atpgs, PDB code: 4dpt:

Fluorine binding site 1 out of 1 in 4dpt

Go back to Fluorine Binding Sites List in 4dpt
Fluorine binding site 1 out of 1 in the Crystal Structure of Staphylococcus Epidermidis Mevalonate Diphosphate Decarboxylase Complexed with Inhibitor 6-Fmvapp and Atpgs


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 Staphylococcus Epidermidis Mevalonate Diphosphate Decarboxylase Complexed with Inhibitor 6-Fmvapp and Atpgs within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F401

b:49.4
occ:0.78
 FAI B:FM0401 0.0 49.4 0.8
CAJ B:FM0401 1.3 36.6 0.8
CAQ B:FM0401 2.4 38.5 0.8
OAE B:FM0401 2.7 36.8 0.8
CAL B:FM0401 2.9 34.7 0.8
N B:ALA284 3.2 34.9 1.0
C B:ASP283 3.5 35.5 1.0
CA B:ASP283 3.6 36.7 1.0
CAM B:FM0401 3.7 31.5 0.8
CZ3 B:TRP19 3.7 34.0 1.0
CB B:ASP283 3.7 37.6 1.0
CE B:MET243 3.8 35.4 1.0
CE3 B:TRP19 3.9 36.8 1.0
OD1 B:ASP283 3.9 43.2 1.0
CA B:ALA284 3.9 30.7 1.0
CB B:ALA284 3.9 40.5 1.0
SD B:MET243 4.0 35.5 1.0
CAK B:FM0401 4.3 35.1 0.8
CG B:ASP283 4.3 42.4 1.0
O B:ASP283 4.4 37.1 1.0
CH2 B:TRP19 4.6 34.3 1.0
O B:TYR18 4.8 27.4 1.0
CAP B:FM0401 4.9 37.8 0.8
CD2 B:TRP19 4.9 27.7 1.0
OAN B:FM0401 4.9 41.8 0.8
CB B:SER192 5.0 49.0 1.0

Reference:

M.L.Barta, W.J.Mcwhorter, H.M.Miziorko, B.V.Geisbrecht. Structural Basis For Nucleotide Binding and Reaction Catalysis in Mevalonate Diphosphate Decarboxylase. Biochemistry V. 51 5611 2012.
ISSN: ISSN 0006-2960
PubMed: 22734632
DOI: 10.1021/BI300591X
Page generated: Thu Aug 1 01:04:21 2024

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