Chlorine in PDB 1cup: Methionine Core Mutant of T4 Lysozyme

All present enzymatic activity of Methionine Core Mutant of T4 Lysozyme:
3.2.1.17;

The structure of Methionine Core Mutant of T4 Lysozyme, PDB code: 1cup was solved by N.C.Gassner, W.A.Baase, J.D.Lindstrom, J.Lu, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.89
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	60.900, 60.900, 97.050, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

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

Chlorine binding site 1 out of 2 in the Methionine Core 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 Methionine Core Mutant of T4 Lysozyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl173 b:33.6 occ:1.00 O A:HOH209 2.9 27.8 1.0 N A:ARG145 3.3 13.8 1.0 N A:ASN144 3.3 6.0 1.0 C A:THR142 3.5 17.3 1.0 CA A:THR142 3.6 8.0 1.0 CB A:THR142 3.6 16.6 1.0 O A:THR142 3.7 14.6 1.0 CB A:ASN144 3.7 12.2 1.0 CA A:ASN144 3.9 15.8 1.0 CB A:ARG145 3.9 8.9 1.0 N A:PRO143 3.9 14.5 1.0 C A:ASN144 4.1 20.0 1.0 CA A:ARG145 4.2 10.2 1.0 CD A:PRO143 4.2 14.1 1.0 C A:PRO143 4.2 13.1 1.0 CG2 A:THR142 4.3 12.8 1.0 CG A:ASN144 4.6 34.3 1.0 O A:HOH230 4.6 32.9 1.0 CA A:PRO143 4.6 11.9 1.0 ND2 A:ASN144 4.8 23.8 1.0 OG1 A:THR142 4.8 15.5 1.0

Chlorine binding site 2 out of 2 in the Methionine Core 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 Methionine Core Mutant of T4 Lysozyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl178 b:42.7 occ:0.50 O A:HOH182 3.4 27.7 1.0 O A:HOH200 3.5 34.5 1.0 O A:HOH246 3.6 45.6 1.0 CE1 A:HIS31 4.2 10.4 1.0 CB A:ALA49 4.2 20.5 1.0 NE2 A:HIS31 4.3 13.9 1.0 NE2 A:GLN69 4.4 19.3 1.0 O A:HOH282 4.6 39.7 1.0 CA A:ALA49 4.7 24.8 1.0 O A:HOH202 4.9 67.0 1.0

N.C.Gassner, W.A.Baase, J.D.Lindstrom, J.Lu, F.W.Dahlquist, B.W.Matthews. Methionine and Alanine Substitutions Show That the Formation of Wild-Type-Like Structure in the Carboxy-Terminal Domain of T4 Lysozyme Is A Rate-Limiting Step in Folding. Biochemistry V. 38 14451 1999.
ISSN: ISSN 0006-2960
PubMed: 10545167
DOI: 10.1021/BI9915519