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Fluorine in PDB 3dmz: Hexafluorobenzene Binding in the Hydrophobic Cavity of T4 Lysozyme L99A Mutant

Enzymatic activity of Hexafluorobenzene Binding in the Hydrophobic Cavity of T4 Lysozyme L99A Mutant

All present enzymatic activity of Hexafluorobenzene Binding in the Hydrophobic Cavity of T4 Lysozyme L99A Mutant:
3.2.1.17;

Protein crystallography data

The structure of Hexafluorobenzene Binding in the Hydrophobic Cavity of T4 Lysozyme L99A Mutant, PDB code: 3dmz was solved by L.Liu, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 51.99 / 2.00
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 59.953, 59.953, 95.491, 90.00, 90.00, 120.00
R / Rfree (%) 17.8 / 21.4

Other elements in 3dmz:

The structure of Hexafluorobenzene Binding in the Hydrophobic Cavity of T4 Lysozyme L99A Mutant also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Hexafluorobenzene Binding in the Hydrophobic Cavity of T4 Lysozyme L99A Mutant (pdb code 3dmz). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 6 binding sites of Fluorine where determined in the Hexafluorobenzene Binding in the Hydrophobic Cavity of T4 Lysozyme L99A Mutant, PDB code: 3dmz:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6;

Fluorine binding site 1 out of 6 in 3dmz

Go back to Fluorine Binding Sites List in 3dmz
Fluorine binding site 1 out of 6 in the Hexafluorobenzene Binding in the Hydrophobic Cavity of T4 Lysozyme L99A Mutant


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Hexafluorobenzene Binding in the Hydrophobic Cavity of T4 Lysozyme L99A Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F900

b:39.0
occ:1.00
F6 A:HFB900 0.0 39.0 1.0
C6 A:HFB900 1.3 39.2 1.0
C5 A:HFB900 2.4 39.4 1.0
C1 A:HFB900 2.4 39.1 1.0
F5 A:HFB900 2.8 39.6 1.0
F1 A:HFB900 2.8 39.2 1.0
CD1 A:LEU121 3.3 17.5 1.0
SD A:MET102 3.5 15.0 1.0
CZ A:PHE153 3.5 16.3 1.0
CD2 A:LEU118 3.6 20.9 1.0
C4 A:HFB900 3.6 39.4 1.0
C2 A:HFB900 3.6 39.3 1.0
CE2 A:PHE153 3.8 16.9 1.0
C3 A:HFB900 4.1 39.3 1.0
CE1 A:PHE153 4.4 16.0 1.0
CE A:MET102 4.4 14.3 1.0
CD2 A:LEU133 4.4 14.3 1.0
CG A:LEU118 4.7 20.2 1.0
F4 A:HFB900 4.7 39.2 1.0
F2 A:HFB900 4.8 38.8 1.0
CD2 A:PHE153 4.8 16.4 1.0
CG A:LEU121 4.8 16.6 1.0

Fluorine binding site 2 out of 6 in 3dmz

Go back to Fluorine Binding Sites List in 3dmz
Fluorine binding site 2 out of 6 in the Hexafluorobenzene Binding in the Hydrophobic Cavity of T4 Lysozyme L99A Mutant


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Hexafluorobenzene Binding in the Hydrophobic Cavity of T4 Lysozyme L99A Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F900

b:39.2
occ:1.00
F1 A:HFB900 0.0 39.2 1.0
C1 A:HFB900 1.3 39.1 1.0
C2 A:HFB900 2.4 39.3 1.0
C6 A:HFB900 2.4 39.2 1.0
F2 A:HFB900 2.7 38.8 1.0
F6 A:HFB900 2.8 39.0 1.0
CD1 A:LEU121 3.2 17.5 1.0
CZ A:PHE153 3.6 16.3 1.0
C3 A:HFB900 3.6 39.3 1.0
C5 A:HFB900 3.6 39.4 1.0
CE1 A:PHE153 3.7 16.0 1.0
CG1 A:VAL87 3.7 19.1 1.0
CD2 A:LEU118 3.7 20.9 1.0
CD1 A:LEU91 3.9 13.9 1.0
CB A:ALA99 4.0 12.3 1.0
C4 A:HFB900 4.1 39.4 1.0
CG A:LEU121 4.4 16.6 1.0
CB A:LEU121 4.5 17.3 1.0
CB A:VAL87 4.6 18.8 1.0
CE2 A:PHE153 4.6 16.9 1.0
CA A:ALA99 4.7 12.4 1.0
F3 A:HFB900 4.7 39.4 1.0
CD1 A:PHE153 4.7 16.2 1.0
F5 A:HFB900 4.8 39.6 1.0
CG A:LEU91 4.9 12.8 1.0

Fluorine binding site 3 out of 6 in 3dmz

Go back to Fluorine Binding Sites List in 3dmz
Fluorine binding site 3 out of 6 in the Hexafluorobenzene Binding in the Hydrophobic Cavity of T4 Lysozyme L99A Mutant


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Hexafluorobenzene Binding in the Hydrophobic Cavity of T4 Lysozyme L99A Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F900

b:39.6
occ:1.00
F5 A:HFB900 0.0 39.6 1.0
C5 A:HFB900 1.3 39.4 1.0
C4 A:HFB900 2.4 39.4 1.0
C6 A:HFB900 2.4 39.2 1.0
F4 A:HFB900 2.7 39.2 1.0
F6 A:HFB900 2.8 39.0 1.0
SD A:MET102 3.3 15.0 1.0
CG1 A:VAL111 3.4 32.9 1.0
CE A:MET102 3.5 14.3 1.0
C3 A:HFB900 3.6 39.3 1.0
C1 A:HFB900 3.6 39.1 1.0
CB A:VAL111 3.8 32.4 1.0
CB A:MET102 3.9 14.5 1.0
C2 A:HFB900 4.1 39.3 1.0
CD2 A:LEU118 4.3 20.9 1.0
CG A:MET102 4.3 14.3 1.0
CG2 A:VAL111 4.6 32.8 1.0
CB A:PHE114 4.7 23.2 1.0
F3 A:HFB900 4.7 39.4 1.0
F1 A:HFB900 4.8 39.2 1.0
CG A:PHE114 4.9 22.3 1.0
O A:ALA99 4.9 12.3 1.0

Fluorine binding site 4 out of 6 in 3dmz

Go back to Fluorine Binding Sites List in 3dmz
Fluorine binding site 4 out of 6 in the Hexafluorobenzene Binding in the Hydrophobic Cavity of T4 Lysozyme L99A Mutant


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Hexafluorobenzene Binding in the Hydrophobic Cavity of T4 Lysozyme L99A Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F900

b:39.2
occ:1.00
F4 A:HFB900 0.0 39.2 1.0
C4 A:HFB900 1.3 39.4 1.0
C5 A:HFB900 2.3 39.4 1.0
C3 A:HFB900 2.4 39.3 1.0
F5 A:HFB900 2.7 39.6 1.0
F3 A:HFB900 2.8 39.4 1.0
CG2 A:VAL103 3.1 16.4 1.0
CD2 A:LEU84 3.4 21.9 1.0
CG2 A:VAL111 3.5 32.8 1.0
CG1 A:VAL111 3.6 32.9 1.0
C6 A:HFB900 3.6 39.2 1.0
C2 A:HFB900 3.6 39.3 1.0
CB A:VAL111 3.7 32.4 1.0
CD1 A:LEU84 3.9 22.4 1.0
C1 A:HFB900 4.1 39.1 1.0
CG A:LEU84 4.2 21.8 1.0
O A:ALA99 4.2 12.3 1.0
CB A:VAL103 4.5 15.9 1.0
F6 A:HFB900 4.7 39.0 1.0
F2 A:HFB900 4.7 38.8 1.0
N A:VAL103 4.8 15.3 1.0
CB A:MET102 4.9 14.5 1.0
CB A:LEU84 4.9 21.9 1.0
CA A:VAL103 4.9 15.8 1.0
CD2 A:LEU118 5.0 20.9 1.0

Fluorine binding site 5 out of 6 in 3dmz

Go back to Fluorine Binding Sites List in 3dmz
Fluorine binding site 5 out of 6 in the Hexafluorobenzene Binding in the Hydrophobic Cavity of T4 Lysozyme L99A Mutant


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of Hexafluorobenzene Binding in the Hydrophobic Cavity of T4 Lysozyme L99A Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F900

b:39.4
occ:1.00
F3 A:HFB900 0.0 39.4 1.0
C3 A:HFB900 1.3 39.3 1.0
C2 A:HFB900 2.4 39.3 1.0
C4 A:HFB900 2.4 39.4 1.0
F2 A:HFB900 2.7 38.8 1.0
F4 A:HFB900 2.8 39.2 1.0
CB A:LEU84 3.5 21.9 1.0
CD2 A:LEU84 3.6 21.9 1.0
C1 A:HFB900 3.6 39.1 1.0
C5 A:HFB900 3.6 39.4 1.0
CG1 A:ILE78 3.7 18.7 1.0
CG2 A:ILE78 3.8 18.0 1.0
CD1 A:ILE78 3.8 18.6 1.0
CG A:LEU84 3.9 21.8 1.0
CD1 A:LEU84 3.9 22.4 1.0
CB A:ALA99 4.1 12.3 1.0
C6 A:HFB900 4.1 39.2 1.0
O A:LEU84 4.2 20.8 1.0
CG2 A:VAL103 4.3 16.4 1.0
CA A:LEU84 4.4 21.9 1.0
CB A:ILE78 4.4 19.0 1.0
C A:LEU84 4.6 21.2 1.0
O A:ALA99 4.6 12.3 1.0
CB A:TYR88 4.7 17.0 1.0
F1 A:HFB900 4.7 39.2 1.0
F5 A:HFB900 4.7 39.6 1.0
CD1 A:TYR88 4.8 17.4 1.0
CA A:ALA99 4.9 12.4 1.0
C A:ALA99 4.9 12.3 1.0

Fluorine binding site 6 out of 6 in 3dmz

Go back to Fluorine Binding Sites List in 3dmz
Fluorine binding site 6 out of 6 in the Hexafluorobenzene Binding in the Hydrophobic Cavity of T4 Lysozyme L99A Mutant


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of Hexafluorobenzene Binding in the Hydrophobic Cavity of T4 Lysozyme L99A Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F900

b:38.8
occ:1.00
F2 A:HFB900 0.0 38.8 1.0
C2 A:HFB900 1.3 39.3 1.0
C3 A:HFB900 2.4 39.3 1.0
C1 A:HFB900 2.4 39.1 1.0
F3 A:HFB900 2.7 39.4 1.0
F1 A:HFB900 2.7 39.2 1.0
CB A:ALA99 3.3 12.3 1.0
N A:TYR88 3.5 17.3 1.0
CA A:TYR88 3.6 17.1 1.0
C4 A:HFB900 3.6 39.4 1.0
C6 A:HFB900 3.6 39.2 1.0
CB A:TYR88 3.7 17.0 1.0
O A:LEU84 4.1 20.8 1.0
CD1 A:LEU91 4.1 13.9 1.0
C A:VAL87 4.1 17.9 1.0
CB A:VAL87 4.1 18.8 1.0
CG1 A:VAL87 4.1 19.1 1.0
C5 A:HFB900 4.1 39.4 1.0
CD1 A:TYR88 4.2 17.4 1.0
CG A:TYR88 4.5 17.5 1.0
CD2 A:LEU118 4.5 20.9 1.0
CA A:ALA99 4.6 12.4 1.0
O A:VAL87 4.7 17.3 1.0
CA A:VAL87 4.7 18.5 1.0
F4 A:HFB900 4.7 39.2 1.0
F6 A:HFB900 4.8 39.0 1.0

Reference:

L.Liu, W.A.Baase, B.W.Matthews. Halogenated Benzenes Bound Within A Non-Polar Cavity in T4 Lysozyme Provide Examples of I...S and I...Se Halogen-Bonding. J.Mol.Biol. V. 385 595 2009.
ISSN: ISSN 0022-2836
PubMed: 19014950
DOI: 10.1016/J.JMB.2008.10.086
Page generated: Wed Jul 31 18:00:59 2024

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