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Bromine in PDB 5jf7: Crystal Structure of Type 2 Pdf From Streptococcus Agalactiae in Complex with Inhibitor SMP289

Enzymatic activity of Crystal Structure of Type 2 Pdf From Streptococcus Agalactiae in Complex with Inhibitor SMP289

All present enzymatic activity of Crystal Structure of Type 2 Pdf From Streptococcus Agalactiae in Complex with Inhibitor SMP289:
3.5.1.88;

Protein crystallography data

The structure of Crystal Structure of Type 2 Pdf From Streptococcus Agalactiae in Complex with Inhibitor SMP289, PDB code: 5jf7 was solved by S.Fieulaine, C.Giglione, T.Meinnel, K.Hamiche, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.66 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 41.470, 65.970, 89.320, 90.00, 90.00, 90.00
R / Rfree (%) 15.4 / 21.1

Other elements in 5jf7:

The structure of Crystal Structure of Type 2 Pdf From Streptococcus Agalactiae in Complex with Inhibitor SMP289 also contains other interesting chemical elements:

Zinc (Zn) 9 atoms

Bromine Binding Sites:

The binding sites of Bromine atom in the Crystal Structure of Type 2 Pdf From Streptococcus Agalactiae in Complex with Inhibitor SMP289 (pdb code 5jf7). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Crystal Structure of Type 2 Pdf From Streptococcus Agalactiae in Complex with Inhibitor SMP289, PDB code: 5jf7:

Bromine binding site 1 out of 1 in 5jf7

Go back to Bromine Binding Sites List in 5jf7
Bromine binding site 1 out of 1 in the Crystal Structure of Type 2 Pdf From Streptococcus Agalactiae in Complex with Inhibitor SMP289


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of Type 2 Pdf From Streptococcus Agalactiae in Complex with Inhibitor SMP289 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br301

b:62.0
occ:1.00
 BR A:6JU301 0.0 62.0 1.0
C8 A:6JU301 1.9 56.5 1.0
C9 A:6JU301 2.9 54.6 1.0
C7 A:6JU301 2.9 57.1 1.0
CD A:GLU129 3.7 19.0 1.0
OE2 A:GLU129 3.8 18.3 1.0
CG2 A:ILE170 3.9 15.1 1.0
CG A:GLU129 3.9 20.5 1.0
CD1 A:LEU125 4.0 19.1 1.0
OE1 A:GLU129 4.0 16.9 1.0
ND1 A:HIS174 4.1 15.8 1.0
C10 A:6JU301 4.2 58.4 1.0
C6 A:6JU301 4.2 63.8 1.0
CB A:HIS174 4.4 13.7 1.0
CG A:HIS174 4.5 15.1 1.0
CB A:GLU129 4.5 21.5 1.0
CG2 A:VAL171 4.5 16.4 1.0
CA A:VAL171 4.6 15.4 1.0
O A:ILE170 4.6 15.5 1.0
C A:ILE170 4.7 15.3 1.0
C11 A:6JU301 4.7 62.8 1.0
N A:VAL171 4.8 16.0 1.0
CE2 A:TYR167 4.9 25.1 1.0
CE1 A:HIS174 4.9 16.1 1.0

Reference:

S.Fieulaine, R.Alves De Sousa, L.Maigre, K.Hamiche, M.Alimi, J.M.Bolla, A.Taleb, A.Denis, J.M.Pages, I.Artaud, T.Meinnel, C.Giglione. A Unique Peptide Deformylase Platform to Rationally Design and Challenge Novel Active Compounds. Sci Rep V. 6 35429 2016.
ISSN: ESSN 2045-2322
PubMed: 27762275
DOI: 10.1038/SREP35429
Page generated: Mon Jul 7 08:32:38 2025

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