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Xenon in PDB 1c6k: T4 Lysozyme Mutant C54T/C97A/L99A in the Presence of 8 Atm Xenon

Enzymatic activity of T4 Lysozyme Mutant C54T/C97A/L99A in the Presence of 8 Atm Xenon

All present enzymatic activity of T4 Lysozyme Mutant C54T/C97A/L99A in the Presence of 8 Atm Xenon:
3.2.1.17;

Protein crystallography data

The structure of T4 Lysozyme Mutant C54T/C97A/L99A in the Presence of 8 Atm Xenon, PDB code: 1c6k 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 (°) 61.068, 61.068, 97.072, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Other elements in 1c6k:

The structure of T4 Lysozyme Mutant C54T/C97A/L99A 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/L99A in the Presence of 8 Atm Xenon (pdb code 1c6k). 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 8 Atm Xenon, PDB code: 1c6k:
Jump to Xenon binding site number: 1; 2; 3;

Xenon binding site 1 out of 3 in 1c6k

Go back to Xenon Binding Sites List in 1c6k
Xenon binding site 1 out of 3 in the T4 Lysozyme Mutant C54T/C97A/L99A 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/L99A in the Presence of 8 Atm Xenon within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Xe500

b:25.8
occ:0.74
XE A:XE502 2.8 47.8 0.1
CB A:ALA99 3.6 11.7 1.0
O A:LEU84 4.0 13.0 1.0
CD2 A:LEU118 4.0 19.3 1.0
N A:TYR88 4.1 13.2 1.0
CG1 A:VAL87 4.1 17.4 1.0
CB A:VAL87 4.1 18.9 1.0
CB A:TYR88 4.2 11.1 1.0
CA A:TYR88 4.3 11.8 1.0
CD2 A:LEU84 4.3 17.7 1.0
CB A:LEU84 4.6 11.7 1.0
C A:VAL87 4.6 11.4 1.0
CA A:LEU84 4.6 16.9 1.0
C A:LEU84 4.7 15.5 1.0
CD1 A:TYR88 4.7 17.4 1.0
CD1 A:LEU91 4.9 16.9 1.0
CA A:ALA99 4.9 11.8 1.0
CA A:VAL87 4.9 12.8 1.0
CG A:TYR88 5.0 18.4 1.0

Xenon binding site 2 out of 3 in 1c6k

Go back to Xenon Binding Sites List in 1c6k
Xenon binding site 2 out of 3 in the T4 Lysozyme Mutant C54T/C97A/L99A 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 2 of T4 Lysozyme Mutant C54T/C97A/L99A in the Presence of 8 Atm Xenon within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Xe501

b:21.7
occ:0.59
XE A:XE502 3.0 47.8 0.1
CD2 A:LEU118 3.6 19.3 1.0
CD1 A:LEU121 3.9 19.9 1.0
SD A:MET102 3.9 20.7 1.0
CG1 A:VAL111 4.0 17.5 1.0
CB A:PHE114 4.1 19.6 1.0
CD2 A:LEU133 4.1 15.3 1.0
CG A:LEU118 4.2 21.6 1.0
CE A:MET102 4.2 19.8 1.0
CB A:SER117 4.3 12.8 1.0
CG A:PHE114 4.6 17.2 1.0
N A:LEU118 4.6 11.8 1.0
O A:VAL111 4.7 16.7 1.0
CD2 A:PHE114 4.7 22.3 1.0
CZ A:PHE153 4.8 15.4 1.0
CA A:LEU118 4.9 15.2 1.0
O A:PHE114 4.9 21.3 1.0
C A:SER117 4.9 13.2 1.0
CE2 A:PHE153 5.0 19.2 1.0

Xenon binding site 3 out of 3 in 1c6k

Go back to Xenon Binding Sites List in 1c6k
Xenon binding site 3 out of 3 in the T4 Lysozyme Mutant C54T/C97A/L99A 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 3 of T4 Lysozyme Mutant C54T/C97A/L99A in the Presence of 8 Atm Xenon within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Xe502

b:47.8
occ:0.12
XE A:XE500 2.8 25.8 0.7
XE A:XE501 3.0 21.7 0.6
CB A:ALA99 3.5 11.7 1.0
CG1 A:VAL111 3.6 17.5 1.0
CD2 A:LEU118 3.8 19.3 1.0
CZ A:PHE153 4.0 15.4 1.0
CA A:ALA99 4.0 11.8 1.0
CD1 A:LEU121 4.4 19.9 1.0
CE1 A:PHE153 4.6 13.2 1.0
SD A:MET102 4.6 20.7 1.0
O A:ALA99 4.8 12.7 1.0
CE2 A:PHE153 4.9 19.2 1.0
C A:ALA99 4.9 10.3 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 02:39:16 2020

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