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Chlorine in PDB 1l93: Similar Hydrophobic Replacements of Leu 99 and Phe 153 Within the Core of T4 Lysozyme Have Different Structural and Thermodynamic Consequences

Enzymatic activity of Similar Hydrophobic Replacements of Leu 99 and Phe 153 Within the Core of T4 Lysozyme Have Different Structural and Thermodynamic Consequences

All present enzymatic activity of Similar Hydrophobic Replacements of Leu 99 and Phe 153 Within the Core of T4 Lysozyme Have Different Structural and Thermodynamic Consequences:
3.2.1.17;

Protein crystallography data

The structure of Similar Hydrophobic Replacements of Leu 99 and Phe 153 Within the Core of T4 Lysozyme Have Different Structural and Thermodynamic Consequences, PDB code: 1l93 was solved by A.E.Eriksson, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.80
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 61.200, 61.200, 96.900, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Similar Hydrophobic Replacements of Leu 99 and Phe 153 Within the Core of T4 Lysozyme Have Different Structural and Thermodynamic Consequences (pdb code 1l93). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Similar Hydrophobic Replacements of Leu 99 and Phe 153 Within the Core of T4 Lysozyme Have Different Structural and Thermodynamic Consequences, PDB code: 1l93:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 1l93

Go back to Chlorine Binding Sites List in 1l93
Chlorine binding site 1 out of 2 in the Similar Hydrophobic Replacements of Leu 99 and Phe 153 Within the Core of T4 Lysozyme Have Different Structural and Thermodynamic Consequences


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Similar Hydrophobic Replacements of Leu 99 and Phe 153 Within the Core of T4 Lysozyme Have Different Structural and Thermodynamic Consequences within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl173

b:32.6
occ:1.00
 O A:HOH209 3.0 24.5 1.0
N A:ARG145 3.3 12.1 1.0
N A:ASN144 3.3 11.3 1.0
C A:THR142 3.5 16.7 1.0
CA A:THR142 3.6 10.6 1.0
CB A:ASN144 3.7 10.7 1.0
O A:THR142 3.7 16.5 1.0
CB A:THR142 3.7 19.5 1.0
CA A:ASN144 3.8 15.4 1.0
N A:PRO143 3.8 16.9 1.0
CB A:ARG145 4.0 13.9 1.0
C A:ASN144 4.0 29.7 1.0
CD A:PRO143 4.1 14.1 1.0
C A:PRO143 4.2 20.8 1.0
CA A:ARG145 4.2 15.9 1.0
CG2 A:THR142 4.4 15.9 1.0
CG A:ASN144 4.5 35.3 1.0
CA A:PRO143 4.6 21.4 1.0
ND2 A:ASN144 4.7 28.3 1.0
OG1 A:THR142 5.0 18.3 1.0
O A:HOH230 5.0 39.0 1.0
N A:THR142 5.0 20.6 1.0

Chlorine binding site 2 out of 2 in 1l93

Go back to Chlorine Binding Sites List in 1l93
Chlorine binding site 2 out of 2 in the Similar Hydrophobic Replacements of Leu 99 and Phe 153 Within the Core of T4 Lysozyme Have Different Structural and Thermodynamic Consequences


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Similar Hydrophobic Replacements of Leu 99 and Phe 153 Within the Core of T4 Lysozyme Have Different Structural and Thermodynamic Consequences within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl178

b:35.0
occ:0.50
 O A:HOH215 3.0 20.7 1.0
O A:HOH182 3.4 21.1 1.0
O A:HOH200 3.5 31.9 1.0
O A:HOH246 3.6 50.6 1.0
CB A:ALA49 4.1 14.9 1.0
CE1 A:HIS31 4.2 17.4 1.0
NE2 A:HIS31 4.3 15.3 1.0
O A:HOH282 4.4 53.9 1.0
NE2 A:GLN69 4.5 13.2 1.0
CA A:ALA49 4.6 25.8 1.0
O A:HOH202 4.7 69.2 1.0
CD2 A:LEU66 4.8 23.9 1.0

Reference:

A.E.Eriksson, W.A.Baase, B.W.Matthews. Similar Hydrophobic Replacements of LEU99 and PHE153 Within the Core of T4 Lysozyme Have Different Structural and Thermodynamic Consequences. J.Mol.Biol. V. 229 747 1993.
ISSN: ISSN 0022-2836
PubMed: 8433369
DOI: 10.1006/JMBI.1993.1077
Page generated: Thu Jul 10 18:00:00 2025

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