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Chlorine in PDB 1xz1: Complex of Halothane with Apoferritin

Protein crystallography data

The structure of Complex of Halothane with Apoferritin, PDB code: 1xz1 was solved by R.Liu, P.J.Loll, R.G.Eckenhoff, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.75
Space group F 4 3 2
Cell size a, b, c (Å), α, β, γ (°) 181.610, 181.610, 181.610, 90.00, 90.00, 90.00
R / Rfree (%) 17.9 / 21.2

Other elements in 1xz1:

The structure of Complex of Halothane with Apoferritin also contains other interesting chemical elements:

Fluorine (F) 3 atoms
Cadmium (Cd) 6 atoms
Bromine (Br) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Complex of Halothane with Apoferritin (pdb code 1xz1). 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 Complex of Halothane with Apoferritin, PDB code: 1xz1:

Chlorine binding site 1 out of 1 in 1xz1

Go back to Chlorine Binding Sites List in 1xz1
Chlorine binding site 1 out of 1 in the Complex of Halothane with Apoferritin


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Complex of Halothane with Apoferritin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl2001

b:45.7
occ:0.50
CL A:HLT2001 0.0 45.7 0.5
C1 A:HLT2001 1.8 48.6 0.5
C2 A:HLT2001 2.7 49.5 0.5
F3 A:HLT2001 2.8 49.7 0.5
BR A:HLT2001 3.0 48.6 0.5
F1 A:HLT2001 3.2 50.8 0.5
CD1 A:TYR28 3.3 14.7 1.0
CG A:TYR28 3.6 12.9 1.0
CB A:TYR28 3.8 12.3 1.0
F2 A:HLT2001 3.9 50.8 0.5
CE1 A:TYR28 3.9 14.7 1.0
CA A:TYR28 4.1 12.4 1.0
CD2 A:TYR28 4.4 13.4 1.0
N A:TYR28 4.6 12.5 1.0
CZ A:TYR28 4.6 13.6 1.0
CD2 A:LEU31 4.7 22.2 1.0
CE2 A:TYR28 4.8 15.1 1.0
CD1 A:LEU81 4.9 25.3 1.0

Reference:

R.Liu, P.J.Loll, R.G.Eckenhoff. Structural Basis For High-Affinity Volatile Anesthetic Binding in A Natural 4-Helix Bundle Protein. Faseb J. V. 19 567 2005.
ISSN: ISSN 0892-6638
PubMed: 15791007
DOI: 10.1096/FJ.04-3171COM
Page generated: Thu Jul 10 20:30:43 2025

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