Chlorine in PDB 5ldm: Crystal Structure of E.Coli Ligt Complexed with 2'-Amp

The structure of Crystal Structure of E.Coli Ligt Complexed with 2'-Amp, PDB code: 5ldm was solved by M.Myllykoski, P.Kursula, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.04 / 2.46
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	108.070, 108.070, 72.640, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 25.3

The binding sites of Chlorine atom in the Crystal Structure of E.Coli Ligt Complexed with 2'-Amp (pdb code 5ldm). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of E.Coli Ligt Complexed with 2'-Amp, PDB code: 5ldm:

Chlorine binding site 1 out of 1 in the Crystal Structure of E.Coli Ligt Complexed with 2'-Amp


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of E.Coli Ligt Complexed with 2'-Amp within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:84.2 occ:1.00 HD22 A:ASN41 2.5 79.4 1.0 H A:ALA38 2.7 76.7 1.0 HA A:VAL37 3.0 72.3 1.0 HG13 A:VAL37 3.1 70.3 1.0 ND2 A:ASN41 3.4 66.2 1.0 N A:ALA38 3.5 63.9 1.0 HB A:THR164 3.6 76.6 1.0 HB2 A:ASN41 3.7 69.8 1.0 HD21 A:ASN41 3.8 79.4 1.0 HB2 A:ALA38 3.8 80.0 1.0 CA A:VAL37 3.9 60.2 1.0 CG1 A:VAL37 4.0 58.6 1.0 HB1 A:ALA38 4.0 80.0 1.0 HH12 A:ARG35 4.0 0.8 1.0 HG22 A:VAL37 4.1 68.9 1.0 HB3 A:ASN41 4.2 69.8 1.0 HG12 A:VAL37 4.2 70.3 1.0 C A:VAL37 4.2 61.9 1.0 CB A:ASN41 4.3 58.1 1.0 CB A:ALA38 4.3 66.7 1.0 CG A:ASN41 4.3 63.6 1.0 HH11 A:ARG35 4.4 0.8 1.0 CB A:VAL37 4.4 58.0 1.0 CB A:THR164 4.5 63.8 1.0 NH1 A:ARG35 4.5 89.9 1.0 CA A:ALA38 4.5 63.4 1.0 H A:THR164 4.5 83.5 1.0 HG11 A:VAL37 4.7 70.3 1.0 CG2 A:VAL37 4.7 57.4 1.0 HG1 A:THR164 4.8 78.5 1.0 HE A:ARG130 4.8 63.0 1.0 O A:PRO36 4.8 60.7 1.0 O A:THR164 4.9 61.4 1.0 HG22 A:THR164 5.0 72.2 1.0

M.Myllykoski, P.Kursula. Structural Aspects of Nucleotide Ligand Binding By A Bacterial 2H Phosphoesterase. Plos One V. 12 70355 2017.
ISSN: ESSN 1932-6203
PubMed: 28141848
DOI: 10.1371/JOURNAL.PONE.0170355