Chlorine in PDB 1d3f: N-Terminal Domain Core Methionine Mutation

All present enzymatic activity of N-Terminal Domain Core Methionine Mutation:
3.2.1.17;

The structure of N-Terminal Domain Core Methionine Mutation, PDB code: 1d3f 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 / 2.05
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	60.970, 60.970, 97.070, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Chlorine atom in the N-Terminal Domain Core Methionine Mutation (pdb code 1d3f). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the N-Terminal Domain Core Methionine Mutation, PDB code: 1d3f:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the N-Terminal Domain Core Methionine Mutation


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of N-Terminal Domain Core Methionine Mutation within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl173 b:30.2 occ:1.00 O A:HOH209 3.0 32.1 1.0 N A:ARG145 3.3 14.8 1.0 N A:ASN144 3.3 3.5 1.0 C A:THR142 3.5 15.8 1.0 CA A:THR142 3.5 9.7 1.0 CB A:THR142 3.6 14.0 1.0 CB A:ASN144 3.6 10.0 1.0 O A:THR142 3.7 17.0 1.0 CA A:ASN144 3.8 12.5 1.0 N A:PRO143 3.8 17.0 1.0 CB A:ARG145 3.9 12.5 1.0 C A:ASN144 4.0 20.2 1.0 CD A:PRO143 4.1 17.6 1.0 CA A:ARG145 4.2 13.2 1.0 C A:PRO143 4.2 6.7 1.0 CG2 A:THR142 4.3 10.8 1.0 CG A:ASN144 4.6 36.4 1.0 CA A:PRO143 4.6 11.0 1.0 ND2 A:ASN144 4.6 28.2 1.0 OG1 A:THR142 4.8 12.8 1.0 N A:THR142 5.0 11.5 1.0 O A:HOH230 5.0 32.8 1.0 CG A:PRO143 5.0 19.8 1.0

Chlorine binding site 2 out of 2 in the N-Terminal Domain Core Methionine Mutation


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of N-Terminal Domain Core Methionine Mutation within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl178 b:39.8 occ:0.50 O A:HOH215 3.0 18.8 1.0 O A:HOH182 3.4 30.3 1.0 O A:HOH246 4.1 50.2 1.0 NE2 A:GLN69 4.2 16.6 1.0 CB A:ALA49 4.3 17.8 1.0 CE1 A:HIS31 4.3 6.2 1.0 O A:HOH200 4.3 46.2 1.0 O A:HOH282 4.5 36.3 1.0 CA A:ALA49 4.6 16.9 1.0 NE2 A:HIS31 4.6 12.6 1.0 O A:HOH202 4.7 62.8 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