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Bromine in PDB 4lu4: Crystal Structure of the N-Terminal Fic Domain of A Putative Cell Filamentation Protein (Virb-Translocated Bep Effector Protein) From Bartonella Quintana

Protein crystallography data

The structure of Crystal Structure of the N-Terminal Fic Domain of A Putative Cell Filamentation Protein (Virb-Translocated Bep Effector Protein) From Bartonella Quintana, PDB code: 4lu4 was solved by Seattle Structural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.92 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 57.560, 43.630, 88.760, 90.00, 91.53, 90.00
R / Rfree (%) 18 / 23.5

Other elements in 4lu4:

The structure of Crystal Structure of the N-Terminal Fic Domain of A Putative Cell Filamentation Protein (Virb-Translocated Bep Effector Protein) From Bartonella Quintana also contains other interesting chemical elements:

Iodine (I) 11 atoms
Chlorine (Cl) 2 atoms

Bromine Binding Sites:

The binding sites of Bromine atom in the Crystal Structure of the N-Terminal Fic Domain of A Putative Cell Filamentation Protein (Virb-Translocated Bep Effector Protein) From Bartonella Quintana (pdb code 4lu4). 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 the N-Terminal Fic Domain of A Putative Cell Filamentation Protein (Virb-Translocated Bep Effector Protein) From Bartonella Quintana, PDB code: 4lu4:

Bromine binding site 1 out of 1 in 4lu4

Go back to Bromine Binding Sites List in 4lu4
Bromine binding site 1 out of 1 in the Crystal Structure of the N-Terminal Fic Domain of A Putative Cell Filamentation Protein (Virb-Translocated Bep Effector Protein) From Bartonella Quintana


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 the N-Terminal Fic Domain of A Putative Cell Filamentation Protein (Virb-Translocated Bep Effector Protein) From Bartonella Quintana within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br302

b:32.6
occ:1.00
O A:HOH419 3.3 12.6 1.0
O A:HOH411 3.6 23.8 1.0
CG A:ARG154 3.8 16.4 1.0
OG1 A:THR34 3.8 21.3 1.0
O A:HOH542 3.9 27.5 1.0
N A:ALA35 4.0 19.1 1.0
CD A:ARG154 4.0 20.1 1.0
CB A:ALA38 4.1 17.4 1.0
O A:THR34 4.1 18.7 1.0
CA A:ALA35 4.1 20.4 1.0
C A:THR34 4.1 19.1 1.0
NE A:ARG154 4.2 22.6 1.0
CB A:ARG154 4.2 13.6 1.0
CB A:THR34 4.4 17.9 1.0
CD1 A:LEU62 4.9 13.8 1.0
CB A:ALA35 4.9 21.1 1.0
CA A:THR34 4.9 18.2 1.0
O A:HOH457 5.0 19.0 1.0

Reference:

D.M.Dranow, J.Abendroth, T.E.Edwards, D.Lorimer. Crystal Structure of the N-Terminal Fic Domain of A Putative Cell Filamentation Protein (Virb-Translocated Bep Effector Protein) From Bartonella Quintana To Be Published.
Page generated: Wed Jul 10 22:00:58 2024

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