Chlorine in PDB 1quo: L99A/E108V Mutant of T4 Lysozyme

All present enzymatic activity of L99A/E108V Mutant of T4 Lysozyme:
3.2.1.17;

The structure of L99A/E108V Mutant of T4 Lysozyme, PDB code: 1quo was solved by J.Wray, W.A.Baase, J.D.Lindstrom, A.R.Poteete, 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 (°)	60.970, 60.970, 97.230, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Chlorine atom in the L99A/E108V Mutant of T4 Lysozyme (pdb code 1quo). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the L99A/E108V Mutant of T4 Lysozyme, PDB code: 1quo:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the L99A/E108V Mutant of T4 Lysozyme


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of L99A/E108V Mutant of T4 Lysozyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl500 b:28.7 occ:1.00 O A:HOH209 3.0 27.9 1.0 N A:ARG145 3.1 12.1 1.0 N A:ASN144 3.2 1.0 1.0 C A:THR142 3.5 12.8 1.0 CB A:THR142 3.6 10.2 1.0 CA A:THR142 3.6 9.2 1.0 CB A:ASN144 3.7 10.0 1.0 CB A:ARG145 3.7 8.5 1.0 CA A:ASN144 3.7 11.6 1.0 O A:THR142 3.7 12.1 1.0 C A:ASN144 3.8 21.8 1.0 N A:PRO143 3.9 15.6 1.0 CA A:ARG145 4.0 12.0 1.0 C A:PRO143 4.1 8.3 1.0 CG2 A:THR142 4.3 14.2 1.0 CD A:PRO143 4.3 11.1 1.0 O A:HOH230 4.4 25.1 1.0 CG A:ASN144 4.6 18.8 1.0 CA A:PRO143 4.6 15.5 1.0 OG1 A:THR142 4.7 10.2 1.0 ND2 A:ASN144 4.7 26.2 1.0 O A:ASN144 4.9 13.3 1.0 O A:HOH228 5.0 36.5 1.0

Chlorine binding site 2 out of 2 in the L99A/E108V Mutant of T4 Lysozyme


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of L99A/E108V Mutant of T4 Lysozyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl501 b:46.1 occ:0.50 O A:HOH215 2.9 14.8 1.0 O A:HOH200 3.4 33.0 1.0 O A:HOH182 3.5 15.7 1.0 O A:HOH244 3.8 41.7 1.0 CB A:ALA49 4.2 8.5 1.0 O A:HOH274 4.3 39.2 1.0 CE1 A:HIS31 4.3 9.3 1.0 NE2 A:GLN69 4.4 12.0 1.0 CA A:ALA49 4.5 16.5 1.0 NE2 A:HIS31 4.5 5.8 1.0 O A:HOH202 4.8 56.1 1.0 CD2 A:LEU66 5.0 15.1 1.0

J.W.Wray, W.A.Baase, J.D.Lindstrom, L.H.Weaver, A.R.Poteete, B.W.Matthews. Structural Analysis of A Non-Contiguous Second-Site Revertant in T4 Lysozyme Shows That Increasing the Rigidity of A Protein Can Enhance Its Stability. J.Mol.Biol. V. 292 1111 1999.
ISSN: ISSN 0022-2836
PubMed: 10512706
DOI: 10.1006/JMBI.1999.3102