Chlorine in PDB 1d3m: Methionine Core Mutation

All present enzymatic activity of Methionine Core Mutation:
3.2.1.17;

The structure of Methionine Core Mutation, PDB code: 1d3m was solved by N.C.Gassner, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.12
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	61.180, 61.180, 96.560, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Chlorine atom in the Methionine Core Mutation (pdb code 1d3m). 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 Mutation, PDB code: 1d3m:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Methionine Core Mutation


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Methionine Core Mutation within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl173 b:31.1 occ:1.00 O A:HOH209 3.0 38.1 1.0 N A:ASN144 3.4 9.7 1.0 N A:ARG145 3.4 9.7 1.0 C A:THR142 3.5 20.6 1.0 CA A:THR142 3.5 10.9 1.0 CB A:THR142 3.6 13.8 1.0 CB A:ASN144 3.8 11.1 1.0 O A:THR142 3.8 18.3 1.0 N A:PRO143 3.8 14.0 1.0 CA A:ASN144 4.0 14.7 1.0 CB A:ARG145 4.1 17.0 1.0 C A:ASN144 4.2 17.2 1.0 CD A:PRO143 4.2 9.9 1.0 CG2 A:THR142 4.2 11.7 1.0 C A:PRO143 4.3 19.3 1.0 CA A:ARG145 4.4 9.9 1.0 CA A:PRO143 4.6 14.9 1.0 CG A:ASN144 4.7 24.8 1.0 O A:HOH245 4.8 45.1 1.0 OG1 A:THR142 4.8 16.2 1.0 O A:HOH230 4.8 46.8 1.0 ND2 A:ASN144 4.8 17.9 1.0 N A:THR142 4.9 12.6 1.0 CG A:PRO143 5.0 13.2 1.0

Chlorine binding site 2 out of 2 in the Methionine Core Mutation


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Methionine Core Mutation within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl178 b:28.8 occ:0.50 O A:HOH215 3.2 26.4 1.0 O A:HOH200 3.3 43.4 1.0 O A:HOH182 3.5 21.8 1.0 O A:HOH246 3.8 49.3 1.0 CB A:ALA49 4.0 20.3 1.0 CE1 A:HIS31 4.1 15.3 1.0 NE2 A:HIS31 4.2 17.2 1.0 O A:HOH282 4.3 35.7 1.0 NE2 A:GLN69 4.6 10.3 1.0 CA A:ALA49 4.7 25.1 1.0 O A:HOH202 4.8 62.4 1.0

N.C.Gassner, B.W.Matthews. Use of Differentially Substituted Selenomethionine Proteins in X-Ray Structure Determination. Acta Crystallogr.,Sect.D V. 55 1967 1999.
ISSN: ISSN 0907-4449
PubMed: 10666571
DOI: 10.1006/JMBI.1999.3220