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Xenon in PDB 1c6t: T4 Lysozyme Mutant C54T/C97A in the Presence of 8 Atm Xenon

Enzymatic activity of T4 Lysozyme Mutant C54T/C97A in the Presence of 8 Atm Xenon

All present enzymatic activity of T4 Lysozyme Mutant C54T/C97A in the Presence of 8 Atm Xenon:
3.2.1.17;

Protein crystallography data

The structure of T4 Lysozyme Mutant C54T/C97A in the Presence of 8 Atm Xenon, PDB code: 1c6t was solved by M.L.Quillin, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 60.00 / 2.00
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 61.006, 61.006, 97.211, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Other elements in 1c6t:

The structure of T4 Lysozyme Mutant C54T/C97A in the Presence of 8 Atm Xenon also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Xenon Binding Sites:

The binding sites of Xenon atom in the T4 Lysozyme Mutant C54T/C97A in the Presence of 8 Atm Xenon (pdb code 1c6t). 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 T4 Lysozyme Mutant C54T/C97A in the Presence of 8 Atm Xenon, PDB code: 1c6t:

Xenon binding site 1 out of 1 in 1c6t

Go back to Xenon Binding Sites List in 1c6t
Xenon binding site 1 out of 1 in the T4 Lysozyme Mutant C54T/C97A in the Presence of 8 Atm Xenon


Mono view


Stereo pair view

A full contact list of Xenon with other atoms in the Xe binding site number 1 of T4 Lysozyme Mutant C54T/C97A in the Presence of 8 Atm Xenon within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Xe500

b:18.1
occ:0.58
CD2 A:LEU118 3.6 16.0 1.0
SD A:MET102 3.9 17.5 1.0
CD2 A:LEU133 4.0 15.2 1.0
CD1 A:LEU121 4.0 23.7 1.0
CB A:PHE114 4.0 22.2 1.0
CG1 A:VAL111 4.1 11.8 1.0
CG A:LEU118 4.1 24.7 1.0
CD1 A:LEU99 4.1 19.2 1.0
CE A:MET102 4.2 17.5 1.0
CB A:SER117 4.2 14.5 1.0
CG A:PHE114 4.5 30.1 1.0
N A:LEU118 4.6 11.9 1.0
CD2 A:PHE114 4.7 36.7 1.0
O A:VAL111 4.7 17.9 1.0
CA A:LEU118 4.8 14.8 1.0
CZ A:PHE153 4.8 16.4 1.0
O A:PHE114 4.9 16.9 1.0
C A:SER117 4.9 15.1 1.0
CE2 A:PHE153 5.0 15.1 1.0

Reference:

M.L.Quillin, W.A.Breyer, I.J.Griswold, B.W.Matthews. Size Versus Polarizability in Protein-Ligand Interactions: Binding of Noble Gases Within Engineered Cavities in Phage T4 Lysozyme. J.Mol.Biol. V. 302 955 2000.
ISSN: ISSN 0022-2836
PubMed: 10993735
DOI: 10.1006/JMBI.2000.4063
Page generated: Wed Dec 16 02:39:19 2020

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