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Xenon in PDB 1c6e: T4 Lysozyme Mutant C54T/C97A/L99A in the Presence of 2 Atm Xenon

Enzymatic activity of T4 Lysozyme Mutant C54T/C97A/L99A in the Presence of 2 Atm Xenon

All present enzymatic activity of T4 Lysozyme Mutant C54T/C97A/L99A in the Presence of 2 Atm Xenon:
3.2.1.17;

Protein crystallography data

The structure of T4 Lysozyme Mutant C54T/C97A/L99A in the Presence of 2 Atm Xenon, PDB code: 1c6e 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 / 1.90
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 61.029, 61.029, 97.271, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Other elements in 1c6e:

The structure of T4 Lysozyme Mutant C54T/C97A/L99A in the Presence of 2 Atm Xenon also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Xenon Binding Sites:

The binding sites of Xenon atom in the T4 Lysozyme Mutant C54T/C97A/L99A in the Presence of 2 Atm Xenon (pdb code 1c6e). This binding sites where shown within 5.0 Angstroms radius around Xenon atom.
In total 3 binding sites of Xenon where determined in the T4 Lysozyme Mutant C54T/C97A/L99A in the Presence of 2 Atm Xenon, PDB code: 1c6e:
Jump to Xenon binding site number: 1; 2; 3;

Xenon binding site 1 out of 3 in 1c6e

Go back to Xenon Binding Sites List in 1c6e
Xenon binding site 1 out of 3 in the T4 Lysozyme Mutant C54T/C97A/L99A in the Presence of 2 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/L99A in the Presence of 2 Atm Xenon within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Xe500

b:24.6
occ:0.41
XE A:XE502 2.6 60.0 0.1
CB A:ALA99 3.7 10.8 1.0
O A:LEU84 3.9 14.9 1.0
CG1 A:VAL87 4.0 18.2 1.0
CD2 A:LEU118 4.1 25.3 1.0
N A:TYR88 4.1 10.1 1.0
CB A:VAL87 4.1 20.0 1.0
CD2 A:LEU84 4.2 29.9 1.0
CB A:TYR88 4.2 14.7 1.0
CA A:TYR88 4.4 11.4 1.0
CB A:LEU84 4.5 8.7 1.0
CA A:LEU84 4.6 14.1 1.0
C A:LEU84 4.6 15.8 1.0
C A:VAL87 4.7 11.8 1.0
CG A:LEU84 4.8 22.8 1.0
CD1 A:TYR88 4.8 18.1 1.0
CA A:ALA99 4.9 10.5 1.0
CA A:VAL87 5.0 13.5 1.0
CG1 A:VAL111 5.0 18.9 1.0

Xenon binding site 2 out of 3 in 1c6e

Go back to Xenon Binding Sites List in 1c6e
Xenon binding site 2 out of 3 in the T4 Lysozyme Mutant C54T/C97A/L99A in the Presence of 2 Atm Xenon


Mono view


Stereo pair view

A full contact list of Xenon with other atoms in the Xe binding site number 2 of T4 Lysozyme Mutant C54T/C97A/L99A in the Presence of 2 Atm Xenon within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Xe501

b:23.1
occ:0.24
XE A:XE502 3.0 60.0 0.1
CD2 A:LEU118 3.4 25.3 1.0
CD1 A:LEU121 3.7 16.3 1.0
SD A:MET102 3.9 19.1 1.0
CG1 A:VAL111 4.0 18.9 1.0
CD2 A:LEU133 4.1 12.5 1.0
CG A:LEU118 4.1 20.3 1.0
CB A:PHE114 4.2 13.4 1.0
CE A:MET102 4.3 16.1 1.0
CB A:SER117 4.4 14.1 1.0
CG A:PHE114 4.6 19.6 1.0
N A:LEU118 4.7 13.3 1.0
CD2 A:PHE114 4.7 22.0 1.0
CZ A:PHE153 4.8 17.7 1.0
O A:VAL111 4.8 16.9 1.0
CA A:LEU118 4.8 17.5 1.0
C A:SER117 5.0 12.4 1.0
CE2 A:PHE153 5.0 16.5 1.0
O A:PHE114 5.0 21.6 1.0

Xenon binding site 3 out of 3 in 1c6e

Go back to Xenon Binding Sites List in 1c6e
Xenon binding site 3 out of 3 in the T4 Lysozyme Mutant C54T/C97A/L99A in the Presence of 2 Atm Xenon


Mono view


Stereo pair view

A full contact list of Xenon with other atoms in the Xe binding site number 3 of T4 Lysozyme Mutant C54T/C97A/L99A in the Presence of 2 Atm Xenon within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Xe502

b:60.0
occ:0.12
XE A:XE500 2.6 24.6 0.4
XE A:XE501 3.0 23.1 0.2
CD2 A:LEU118 3.2 25.3 1.0
CG1 A:VAL111 3.3 18.9 1.0
CB A:ALA99 4.0 10.8 1.0
CA A:ALA99 4.4 10.5 1.0
CZ A:PHE153 4.5 17.7 1.0
CD1 A:LEU121 4.6 16.3 1.0
CD2 A:LEU84 4.7 29.9 1.0
CG A:LEU118 4.7 20.3 1.0
CB A:VAL111 4.8 19.7 1.0
SD A:MET102 4.9 19.1 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 02:39:17 2020

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