Chlorine in PDB 1qud: L99G Mutant of T4 Lysozyme

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

The structure of L99G Mutant of T4 Lysozyme, PDB code: 1qud 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 / 1.75
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	60.990, 60.990, 97.060, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Chlorine atom in the L99G Mutant of T4 Lysozyme (pdb code 1qud). 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 Mutant of T4 Lysozyme, PDB code: 1qud:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the L99G 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 Mutant of T4 Lysozyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl500 b:65.2 occ:1.00 N A:ARG145 2.9 10.6 1.0 O A:HOH209 3.2 50.8 1.0 N A:ASN144 3.2 7.9 1.0 CB A:ARG145 3.4 17.6 1.0 C A:THR142 3.4 14.7 1.0 O A:THR142 3.5 12.9 1.0 CB A:ASN144 3.6 15.0 1.0 CB A:THR142 3.6 16.0 1.0 CA A:ASN144 3.6 11.8 1.0 CA A:THR142 3.6 9.8 1.0 C A:ASN144 3.7 20.2 1.0 CA A:ARG145 3.7 10.3 1.0 N A:PRO143 3.9 15.0 1.0 C A:PRO143 4.1 14.9 1.0 O A:HOH227 4.3 33.9 1.0 CG2 A:THR142 4.4 12.8 1.0 CD A:PRO143 4.5 12.8 1.0 CA A:PRO143 4.6 14.4 1.0 CG A:ASN144 4.6 34.1 1.0 OG1 A:THR142 4.7 18.2 1.0 N A:ALA146 4.8 11.5 1.0 O A:ASN144 4.9 15.5 1.0 CG A:ARG145 4.9 16.8 1.0 C A:ARG145 4.9 13.1 1.0 O A:PRO143 5.0 13.0 1.0

Chlorine binding site 2 out of 2 in the L99G 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 Mutant of T4 Lysozyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl501 b:48.6 occ:0.50 O A:HOH215 2.9 23.3 1.0 O A:HOH182 3.4 24.4 1.0 O A:HOH237 3.8 64.0 0.0 CB A:ALA49 4.0 19.9 1.0 O A:HOH200 4.2 39.4 1.0 CE1 A:HIS31 4.3 10.1 1.0 NE2 A:GLN69 4.3 18.4 1.0 CA A:ALA49 4.3 20.3 1.0 O A:HOH253 4.4 32.7 1.0 NE2 A:HIS31 4.4 15.6 1.0 CD2 A:LEU66 4.6 20.9 1.0 O A:ALA49 4.8 11.2 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