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Chlorine in PDB 234l: T4 Lysozyme Mutant M106L

Enzymatic activity of T4 Lysozyme Mutant M106L

All present enzymatic activity of T4 Lysozyme Mutant M106L:
3.2.1.17;

Protein crystallography data

The structure of T4 Lysozyme Mutant M106L, PDB code: 234l was solved by L.A.Lipscomb, D.L.Drew, N.Gassner, W.A.Baase, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.90
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 60.890, 60.890, 97.170, 90.00, 90.00, 120.00
R / Rfree (%) 17.1 / n/a

Chlorine Binding Sites:

The binding sites of Chlorine atom in the T4 Lysozyme Mutant M106L (pdb code 234l). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the T4 Lysozyme Mutant M106L, PDB code: 234l:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 234l

Go back to Chlorine Binding Sites List in 234l
Chlorine binding site 1 out of 2 in the T4 Lysozyme Mutant M106L


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of T4 Lysozyme Mutant M106L within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl173

b:26.4
occ:1.00
O A:HOH209 3.1 28.6 1.0
N A:ARG145 3.2 7.1 1.0
N A:ASN144 3.2 3.7 1.0
C A:THR142 3.6 16.8 1.0
CB A:ASN144 3.6 11.0 1.0
CA A:THR142 3.6 8.9 1.0
CA A:ASN144 3.7 9.7 1.0
CB A:THR142 3.8 12.6 1.0
O A:THR142 3.8 10.2 1.0
N A:PRO143 3.9 16.9 1.0
C A:ASN144 4.0 14.0 1.0
CB A:ARG145 4.1 17.1 1.0
CD A:PRO143 4.1 16.4 1.0
C A:PRO143 4.2 12.7 1.0
CA A:ARG145 4.2 9.0 1.0
CG A:ASN144 4.4 28.7 1.0
CG2 A:THR142 4.4 7.5 1.0
ND2 A:ASN144 4.5 35.7 1.0
CA A:PRO143 4.6 9.7 1.0
O A:HOH543 4.9 27.2 1.0
OG1 A:THR142 4.9 11.1 1.0

Chlorine binding site 2 out of 2 in 234l

Go back to Chlorine Binding Sites List in 234l
Chlorine binding site 2 out of 2 in the T4 Lysozyme Mutant M106L


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of T4 Lysozyme Mutant M106L within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl178

b:34.3
occ:0.50
O A:HOH215 3.0 13.4 1.0
O A:HOH182 3.3 20.2 1.0
O A:HOH556 3.5 47.9 1.0
O A:HOH536 3.6 38.5 1.0
CE1 A:HIS31 3.9 11.2 1.0
NE2 A:HIS31 4.2 10.0 1.0
CB A:ALA49 4.2 10.0 1.0
NE2 A:GLN69 4.4 17.4 1.0
O A:HOH546 4.4 31.4 1.0
CA A:ALA49 4.6 11.5 1.0
CD2 A:LEU66 4.8 15.0 1.0

Reference:

L.A.Lipscomb, N.C.Gassner, S.D.Snow, A.M.Eldridge, W.A.Baase, D.L.Drew, B.W.Matthews. Context-Dependent Protein Stabilization By Methionine-to-Leucine Substitution Shown in T4 Lysozyme. Protein Sci. V. 7 765 1998.
ISSN: ISSN 0961-8368
PubMed: 9541409
Page generated: Sat Jul 20 04:58:13 2024

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