Chlorine in PDB 1d3n: Methionine Core Mutation

All present enzymatic activity of Methionine Core Mutation:
3.2.1.17;

The structure of Methionine Core Mutation, PDB code: 1d3n 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 / 2.00
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	61.260, 61.260, 96.590, 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 1d3n). 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: 1d3n:
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:49.7 occ:1.00 O A:HOH209 2.9 39.4 1.0 N A:ARG145 3.2 12.5 1.0 N A:ASN144 3.4 7.2 1.0 C A:THR142 3.5 21.0 1.0 CA A:THR142 3.6 4.3 1.0 CB A:THR142 3.7 12.8 1.0 CB A:ARG145 3.8 11.9 1.0 CB A:ASN144 3.8 14.2 1.0 O A:THR142 3.8 14.7 1.0 N A:PRO143 3.9 18.1 1.0 CA A:ASN144 3.9 15.8 1.0 CA A:ARG145 4.1 12.9 1.0 C A:ASN144 4.1 29.3 1.0 C A:PRO143 4.2 21.2 1.0 CD A:PRO143 4.4 19.6 1.0 CG A:ASN144 4.5 32.6 1.0 CG2 A:THR142 4.5 19.1 1.0 ND2 A:ASN144 4.5 44.1 1.0 CA A:PRO143 4.6 17.9 1.0 O A:HOH230 4.7 30.4 1.0 O A:HOH245 4.7 42.9 1.0 OG1 A:THR142 4.8 18.8 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:38.6 occ:0.50 O A:HOH215 3.2 15.6 1.0 O A:HOH182 3.4 21.2 1.0 O A:HOH200 3.6 35.9 1.0 CE1 A:HIS31 4.1 17.6 1.0 O A:HOH246 4.1 74.0 1.0 CB A:ALA49 4.1 11.3 1.0 O A:HOH202 4.2 50.7 1.0 NE2 A:HIS31 4.3 23.4 1.0 NE2 A:GLN69 4.5 13.7 1.0 CA A:ALA49 4.9 16.9 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