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Chlorine in PDB 1g1w: T4 Lysozyme Mutant C54T/C97A/Q105M

Enzymatic activity of T4 Lysozyme Mutant C54T/C97A/Q105M

All present enzymatic activity of T4 Lysozyme Mutant C54T/C97A/Q105M:
3.2.1.17;

Protein crystallography data

The structure of T4 Lysozyme Mutant C54T/C97A/Q105M, PDB code: 1g1w 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) 30.00 / 1.80
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 61.093, 61.093, 96.857, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Chlorine Binding Sites:

The binding sites of Chlorine atom in the T4 Lysozyme Mutant C54T/C97A/Q105M (pdb code 1g1w). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the T4 Lysozyme Mutant C54T/C97A/Q105M, PDB code: 1g1w:

Chlorine binding site 1 out of 1 in 1g1w

Go back to Chlorine Binding Sites List in 1g1w
Chlorine binding site 1 out of 1 in the T4 Lysozyme Mutant C54T/C97A/Q105M


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 C54T/C97A/Q105M within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl173

b:48.5
occ:1.00
N A:ARG145 3.0 9.8 1.0
O A:HOH209 3.0 40.1 1.0
N A:ASN144 3.4 5.2 1.0
CB A:THR142 3.5 16.6 1.0
CB A:ARG145 3.5 16.7 1.0
C A:THR142 3.5 11.6 1.0
O A:THR142 3.6 10.6 1.0
CA A:THR142 3.6 8.0 1.0
CA A:ASN144 3.7 9.6 1.0
CB A:ASN144 3.8 9.8 1.0
CA A:ARG145 3.8 9.5 1.0
C A:ASN144 3.8 15.3 1.0
CG2 A:THR142 4.0 17.6 1.0
N A:PRO143 4.0 13.8 1.0
C A:PRO143 4.3 9.1 1.0
CD A:PRO143 4.4 15.4 1.0
OG1 A:THR142 4.7 16.8 1.0
CG A:ARG145 4.8 21.4 1.0
CA A:PRO143 4.8 9.1 1.0
N A:ALA146 4.8 7.5 1.0
CG A:ASN144 4.9 38.4 1.0
C A:ARG145 4.9 12.7 1.0

Reference:

J.Xu, W.A.Baase, M.L.Quillin, E.P.Baldwin, B.W.Matthews. Structural and Thermodynamic Analysis of the Binding of Solvent at Internal Sites in T4 Lysozyme. Protein Sci. V. 10 1067 2001.
ISSN: ISSN 0961-8368
PubMed: 11316887
DOI: 10.1110/PS.02101
Page generated: Sat Dec 12 08:35:44 2020

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