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Xenon in PDB 2zfe: Crystal Structure of Bacteriorhodopsin-Xenon Complex

Protein crystallography data

The structure of Crystal Structure of Bacteriorhodopsin-Xenon Complex, PDB code: 2zfe was solved by T.Kouyama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 2.50
Space group P 6 2 2
Cell size a, b, c (Å), α, β, γ (°) 102.410, 102.410, 112.470, 90.00, 90.00, 120.00
R / Rfree (%) 25 / 27.9

Xenon Binding Sites:

The binding sites of Xenon atom in the Crystal Structure of Bacteriorhodopsin-Xenon Complex (pdb code 2zfe). This binding sites where shown within 5.0 Angstroms radius around Xenon atom.
In total only one binding site of Xenon was determined in the Crystal Structure of Bacteriorhodopsin-Xenon Complex, PDB code: 2zfe:

Xenon binding site 1 out of 1 in 2zfe

Go back to Xenon Binding Sites List in 2zfe
Xenon binding site 1 out of 1 in the Crystal Structure of Bacteriorhodopsin-Xenon Complex


Mono view


Stereo pair view

A full contact list of Xenon with other atoms in the Xe binding site number 1 of Crystal Structure of Bacteriorhodopsin-Xenon Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Xe638

b:44.2
occ:0.29
CG2 A:ILE108 3.4 32.6 1.0
CG2 A:VAL112 3.6 36.9 1.0
N A:LEU95 3.6 37.5 1.0
CB A:LEU94 3.7 38.7 1.0
C A:LEU94 3.7 37.3 1.0
O A:ILE108 3.8 36.9 1.0
CA A:LEU95 3.8 37.4 1.0
O A:HOH639 3.9 45.7 0.2
O A:LEU94 4.0 36.6 1.0
CA A:ILE108 4.1 35.9 1.0
CB A:ILE108 4.2 36.1 1.0
CD1 A:LEU95 4.2 38.0 1.0
CB A:LEU111 4.3 36.8 1.0
CB A:ALA98 4.3 34.0 1.0
C A:ILE108 4.3 36.8 1.0
CA A:LEU94 4.4 37.1 1.0
O A:PRO91 4.4 32.8 1.0
CB A:LEU95 4.4 38.8 1.0
CG1 A:ILE108 4.4 32.6 1.0
CG A:LEU94 4.5 40.3 1.0
N A:VAL112 4.6 34.6 1.0
CB A:VAL112 4.9 35.9 1.0
CD2 A:LEU94 5.0 40.5 1.0

Reference:

N.Hayakawa, T.Kasahara, D.Hasegawa, K.Yoshimura, M.Murakami, T.Kouyama. Effect of Xenon Binding to A Hydrophobic Cavity on the Proton Pumping Cycle in Bacteriorhodopsin J.Mol.Biol. V. 384 812 2008.
ISSN: ISSN 0022-2836
PubMed: 18930734
DOI: 10.1016/J.JMB.2008.09.075
Page generated: Wed Dec 16 02:39:43 2020

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