Chlorine in PDB 1d2y: 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: 1d2y 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 / 2.06
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	61.090, 61.090, 97.430, 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 1d2y). 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: 1d2y:
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:31.3 occ:1.00 O A:HOH209 3.0 41.6 1.0 N A:ASN144 3.2 4.3 1.0 N A:ARG145 3.3 14.3 1.0 C A:THR142 3.5 19.3 1.0 CA A:THR142 3.5 14.1 1.0 CB A:THR142 3.7 26.9 1.0 O A:THR142 3.7 14.5 1.0 CB A:ASN144 3.8 14.7 1.0 N A:PRO143 3.8 18.2 1.0 CA A:ASN144 3.8 10.1 1.0 CB A:ARG145 4.0 11.5 1.0 CD A:PRO143 4.1 13.4 1.0 C A:ASN144 4.1 16.6 1.0 C A:PRO143 4.2 20.5 1.0 CA A:ARG145 4.3 13.3 1.0 CG2 A:THR142 4.4 17.9 1.0 ND2 A:ASN144 4.5 30.7 1.0 CA A:PRO143 4.5 19.5 1.0 CG A:ASN144 4.5 27.9 1.0 CG A:PRO143 4.9 11.8 1.0 OG1 A:THR142 4.9 16.2 1.0 N A:THR142 4.9 14.9 1.0 O A:HOH230 5.0 51.4 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:53.0 occ:0.50 O A:HOH215 3.3 24.9 1.0 O A:HOH200 3.6 37.1 1.0 O A:HOH182 3.7 26.8 1.0 CE1 A:HIS31 4.3 12.4 1.0 O A:HOH282 4.4 32.7 1.0 NE2 A:HIS31 4.4 11.8 1.0 NE2 A:GLN69 4.7 14.3 1.0 CB A:ALA49 4.7 20.0 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