Chlorine in PDB 1g0g: Crystal Structure of T4 Lysozyme Mutant T152A

All present enzymatic activity of Crystal Structure of T4 Lysozyme Mutant T152A:
3.2.1.17;

The structure of Crystal Structure of T4 Lysozyme Mutant T152A, PDB code: 1g0g was solved by J.Xu, W.A.Baase, 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)	10.00 / 1.90
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	60.820, 60.820, 96.990, 90.00, 90.00, 120.00
R / Rfree (%)	15.4 / n/a

The binding sites of Chlorine atom in the Crystal Structure of T4 Lysozyme Mutant T152A (pdb code 1g0g). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of T4 Lysozyme Mutant T152A, PDB code: 1g0g:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of T4 Lysozyme Mutant T152A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of T4 Lysozyme Mutant T152A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl173 b:33.5 occ:1.00 O A:HOH209 3.0 28.7 1.0 N A:ARG145 3.2 14.8 1.0 N A:ASN144 3.3 8.3 1.0 C A:THR142 3.5 18.3 1.0 CA A:THR142 3.5 10.6 1.0 CB A:THR142 3.6 16.4 1.0 CB A:ASN144 3.6 10.5 1.0 O A:THR142 3.7 14.8 1.0 CA A:ASN144 3.8 14.6 1.0 N A:PRO143 3.9 18.5 1.0 CB A:ARG145 3.9 16.0 1.0 C A:ASN144 4.0 23.1 1.0 CA A:ARG145 4.1 16.6 1.0 CD A:PRO143 4.2 14.9 1.0 C A:PRO143 4.3 14.2 1.0 CG2 A:THR142 4.3 13.6 1.0 CG A:ASN144 4.6 30.7 1.0 CA A:PRO143 4.6 16.0 1.0 O A:HOH230 4.7 39.0 1.0 O A:HOH327 4.7 60.7 1.0 ND2 A:ASN144 4.8 28.1 1.0 OG1 A:THR142 4.8 18.6 1.0 N A:THR142 4.9 14.6 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of T4 Lysozyme Mutant T152A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of T4 Lysozyme Mutant T152A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl178 b:39.1 occ:0.50 O A:HOH215 3.0 21.9 1.0 O A:HOH182 3.1 24.0 1.0 O A:HOH200 3.7 31.9 1.0 O A:HOH246 3.8 51.6 1.0 CE1 A:HIS31 4.1 15.9 1.0 CB A:ALA49 4.1 18.4 1.0 NE2 A:GLN69 4.3 15.8 1.0 NE2 A:HIS31 4.3 14.3 1.0 O A:HOH202 4.5 71.5 1.0 O A:HOH282 4.5 41.8 1.0 CA A:ALA49 4.7 20.7 1.0 CD2 A:LEU66 4.8 22.1 1.0

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