Chlorine in PDB 1quh: L99G/E108V Mutant of T4 Lysozyme

All present enzymatic activity of L99G/E108V Mutant of T4 Lysozyme:
3.2.1.17;

The structure of L99G/E108V Mutant of T4 Lysozyme, PDB code: 1quh 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)	19.00 / 1.85
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	61.000, 61.000, 97.100, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Chlorine atom in the L99G/E108V Mutant of T4 Lysozyme (pdb code 1quh). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the L99G/E108V Mutant of T4 Lysozyme, PDB code: 1quh:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the L99G/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 L99G/E108V Mutant of T4 Lysozyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl500 b:34.5 occ:1.00 O A:HOH209 2.8 33.4 1.0 O A:HOH285 3.0 32.5 1.0 N A:ARG145 3.2 9.9 1.0 N A:ASN144 3.3 11.3 1.0 C A:THR142 3.4 11.9 1.0 CB A:THR142 3.5 8.8 1.0 CA A:THR142 3.6 4.7 1.0 O A:THR142 3.7 15.4 1.0 CB A:ASN144 3.8 16.5 1.0 CB A:ARG145 3.8 22.1 1.0 N A:PRO143 3.8 17.3 1.0 CA A:ASN144 3.8 6.8 1.0 C A:ASN144 4.0 18.4 1.0 CA A:ARG145 4.1 1.1 1.0 C A:PRO143 4.1 8.6 1.0 CG2 A:THR142 4.2 12.1 1.0 CD A:PRO143 4.3 14.7 1.0 O A:HOH230 4.5 21.2 1.0 CA A:PRO143 4.5 9.8 1.0 CG A:ASN144 4.6 30.8 1.0 OG1 A:THR142 4.7 12.4 1.0 ND2 A:ASN144 4.9 40.9 1.0

Chlorine binding site 2 out of 2 in the L99G/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 L99G/E108V Mutant of T4 Lysozyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl501 b:49.8 occ:0.50 O A:HOH215 3.0 17.6 1.0 CB A:ALA49 3.5 15.6 1.0 O A:HOH182 3.7 25.1 1.0 O A:HOH256 4.0 39.4 1.0 CA A:ALA49 4.1 17.5 1.0 NE2 A:HIS31 4.3 13.2 1.0 CE1 A:HIS31 4.3 8.5 1.0 CD2 A:LEU66 4.5 18.9 1.0 NE2 A:GLN69 4.6 13.5 1.0 O A:ALA49 4.7 9.2 1.0 O A:HOH200 4.7 57.8 1.0 C A:ALA49 4.9 11.4 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