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Chlorine in PDB 3bfb: Crystal Structure of A Pheromone Binding Protein From Apis Mellifera in Complex with the 9-Keto-2(E)-Decenoic Acid

Protein crystallography data

The structure of Crystal Structure of A Pheromone Binding Protein From Apis Mellifera in Complex with the 9-Keto-2(E)-Decenoic Acid, PDB code: 3bfb was solved by M.E.Pesenti, S.Spinelli, V.Bezirard, L.Briand, J.C.Pernollet, M.Tegoni, C.Cambillau, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 2.15
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 78.099, 84.281, 47.602, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 25.2

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of A Pheromone Binding Protein From Apis Mellifera in Complex with the 9-Keto-2(E)-Decenoic Acid (pdb code 3bfb). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of A Pheromone Binding Protein From Apis Mellifera in Complex with the 9-Keto-2(E)-Decenoic Acid, PDB code: 3bfb:

Chlorine binding site 1 out of 1 in 3bfb

Go back to Chlorine Binding Sites List in 3bfb
Chlorine binding site 1 out of 1 in the Crystal Structure of A Pheromone Binding Protein From Apis Mellifera in Complex with the 9-Keto-2(E)-Decenoic Acid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of A Pheromone Binding Protein From Apis Mellifera in Complex with the 9-Keto-2(E)-Decenoic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl120

b:51.3
occ:0.50
O A:HOH181 3.2 57.3 0.5
CE A:LYS100 4.3 46.5 0.5
O A:GLY94 4.4 51.0 1.0
NZ A:LYS100 4.4 46.0 0.5

Reference:

M.E.Pesenti, S.Spinelli, V.Bezirard, L.Briand, J.C.Pernollet, M.Tegoni, C.Cambillau. Structural Basis of the Honey Bee Pbp Pheromone and pH-Induced Conformational Change J.Mol.Biol. V. 380 158 2008.
ISSN: ISSN 0022-2836
PubMed: 18508083
DOI: 10.1016/J.JMB.2008.04.048
Page generated: Sat Dec 12 09:33:09 2020

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