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Chlorine in PDB 1l76: Tolerance of T4 Lysozyme to Proline Substitutions Within the Long Interdomain Alpha-Helix Illustrates the Adaptability of Proteins to Potentially Destabilizing Lesions

Enzymatic activity of Tolerance of T4 Lysozyme to Proline Substitutions Within the Long Interdomain Alpha-Helix Illustrates the Adaptability of Proteins to Potentially Destabilizing Lesions

All present enzymatic activity of Tolerance of T4 Lysozyme to Proline Substitutions Within the Long Interdomain Alpha-Helix Illustrates the Adaptability of Proteins to Potentially Destabilizing Lesions:
3.2.1.17;

Protein crystallography data

The structure of Tolerance of T4 Lysozyme to Proline Substitutions Within the Long Interdomain Alpha-Helix Illustrates the Adaptability of Proteins to Potentially Destabilizing Lesions, PDB code: 1l76 was solved by U.Sauer, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.90
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 60.770, 60.770, 98.620, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Tolerance of T4 Lysozyme to Proline Substitutions Within the Long Interdomain Alpha-Helix Illustrates the Adaptability of Proteins to Potentially Destabilizing Lesions (pdb code 1l76). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Tolerance of T4 Lysozyme to Proline Substitutions Within the Long Interdomain Alpha-Helix Illustrates the Adaptability of Proteins to Potentially Destabilizing Lesions, PDB code: 1l76:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 1l76

Go back to Chlorine Binding Sites List in 1l76
Chlorine binding site 1 out of 2 in the Tolerance of T4 Lysozyme to Proline Substitutions Within the Long Interdomain Alpha-Helix Illustrates the Adaptability of Proteins to Potentially Destabilizing Lesions


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Tolerance of T4 Lysozyme to Proline Substitutions Within the Long Interdomain Alpha-Helix Illustrates the Adaptability of Proteins to Potentially Destabilizing Lesions within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl173

b:30.4
occ:1.00
 N A:ARG145 3.3 12.2 1.0
N A:ASN144 3.3 10.4 1.0
O A:HOH209 3.3 43.8 1.0
C A:THR142 3.4 21.0 1.0
CA A:THR142 3.4 9.1 1.0
CB A:THR142 3.6 14.7 1.0
CB A:ASN144 3.6 21.5 1.0
CA A:ASN144 3.7 13.4 1.0
O A:THR142 3.7 16.3 1.0
N A:PRO143 3.9 12.9 1.0
CB A:ARG145 3.9 13.1 1.0
C A:ASN144 4.0 23.0 1.0
CA A:ARG145 4.2 10.7 1.0
C A:PRO143 4.2 15.3 1.0
CD A:PRO143 4.3 9.3 1.0
CG2 A:THR142 4.3 12.2 1.0
O A:HOH245 4.4 56.8 1.0
CG A:ASN144 4.6 22.7 1.0
CA A:PRO143 4.6 11.6 1.0
ND2 A:ASN144 4.7 27.5 1.0
N A:THR142 4.8 8.4 1.0
OG1 A:THR142 4.8 11.5 1.0
O A:HOH230 4.8 28.9 1.0
CG A:PRO143 5.0 9.3 1.0

Chlorine binding site 2 out of 2 in 1l76

Go back to Chlorine Binding Sites List in 1l76
Chlorine binding site 2 out of 2 in the Tolerance of T4 Lysozyme to Proline Substitutions Within the Long Interdomain Alpha-Helix Illustrates the Adaptability of Proteins to Potentially Destabilizing Lesions


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Tolerance of T4 Lysozyme to Proline Substitutions Within the Long Interdomain Alpha-Helix Illustrates the Adaptability of Proteins to Potentially Destabilizing Lesions within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl178

b:31.5
occ:0.50
 O A:HOH182 3.0 16.2 1.0
O A:HOH215 3.0 15.9 1.0
O A:HOH246 3.5 40.1 1.0
O A:HOH200 3.6 38.6 1.0
CE1 A:HIS31 4.0 8.7 1.0
CB A:ALA49 4.2 30.5 1.0
NE2 A:GLN69 4.3 12.1 1.0
NE2 A:HIS31 4.3 19.2 1.0
CA A:ALA49 4.7 24.1 1.0
CD2 A:LEU66 4.8 12.2 1.0

Reference:

U.H.Sauer, D.P.San, B.W.Matthews. Tolerance of T4 Lysozyme to Proline Substitutions Within the Long Interdomain Alpha-Helix Illustrates the Adaptability of Proteins to Potentially Destabilizing Lesions. J.Biol.Chem. V. 267 2393 1992.
ISSN: ISSN 0021-9258
PubMed: 1733941
Page generated: Thu Jul 10 17:58:19 2025

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