Chlorine in PDB 5ao9: The Structure of A Novel Thermophilic Esterase From the Planctomycetes Species, Thermogutta Terrifontis, EST2-Native

All present enzymatic activity of The Structure of A Novel Thermophilic Esterase From the Planctomycetes Species, Thermogutta Terrifontis, EST2-Native:
3.1.1.1;

The structure of The Structure of A Novel Thermophilic Esterase From the Planctomycetes Species, Thermogutta Terrifontis, EST2-Native, PDB code: 5ao9 was solved by C.Sayer, Z.Szabo, M.N.Isupov, C.Ingham, J.A.Littlechild, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.83 / 1.58
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	61.640, 71.070, 75.840, 90.00, 90.00, 90.00
R / Rfree (%)	15 / 17.5

The binding sites of Chlorine atom in the The Structure of A Novel Thermophilic Esterase From the Planctomycetes Species, Thermogutta Terrifontis, EST2-Native (pdb code 5ao9). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the The Structure of A Novel Thermophilic Esterase From the Planctomycetes Species, Thermogutta Terrifontis, EST2-Native, PDB code: 5ao9:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the The Structure of A Novel Thermophilic Esterase From the Planctomycetes Species, Thermogutta Terrifontis, EST2-Native


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The Structure of A Novel Thermophilic Esterase From the Planctomycetes Species, Thermogutta Terrifontis, EST2-Native within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1298 b:31.6 occ:0.80 N A:ASN217 3.1 26.7 1.0 O A:HOH2186 3.3 52.5 1.0 N A:HIS248 3.4 22.5 1.0 OG1 A:THR218 3.5 31.3 1.0 CB A:HIS248 3.6 21.9 1.0 N A:THR218 3.7 24.8 1.0 CB A:ALA247 3.7 35.1 1.0 CB A:ASN217 3.8 36.9 1.0 OD1 A:ASP216 3.8 21.7 1.0 CA A:ASN217 3.8 33.7 1.0 O A:HOH2163 3.8 58.3 1.0 C A:ASP216 4.1 22.3 1.0 CA A:ASP216 4.1 23.7 1.0 C A:ASN217 4.1 37.8 1.0 CA A:HIS248 4.1 21.8 1.0 CA A:ALA247 4.3 25.4 1.0 C A:ALA247 4.3 21.6 1.0 CB A:THR218 4.3 28.5 1.0 O A:ALA215 4.4 28.9 1.0 CG A:ASP216 4.5 23.4 1.0 ND2 A:ASN217 4.5 51.2 1.0 CG A:ASN217 4.6 50.9 1.0 CA A:THR218 4.7 24.4 1.0 CG A:HIS248 4.9 21.1 1.0 CB A:ASP216 4.9 21.5 1.0 O A:HIS248 4.9 26.9 1.0

Chlorine binding site 2 out of 2 in the The Structure of A Novel Thermophilic Esterase From the Planctomycetes Species, Thermogutta Terrifontis, EST2-Native


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of The Structure of A Novel Thermophilic Esterase From the Planctomycetes Species, Thermogutta Terrifontis, EST2-Native within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1299 b:44.4 occ:0.70 O A:HOH2176 1.8 31.5 0.3 O A:HOH2156 3.2 21.8 1.0 NH1 A:ARG237 3.2 44.2 0.4 CB A:ARG237 4.2 22.2 0.6 CB A:ARG237 4.3 24.3 0.4 CB A:PRO207 4.4 17.4 1.0 CZ A:ARG237 4.5 42.0 0.4 O A:HOH2204 4.5 59.7 1.0 CD A:PRO207 4.5 18.5 1.0 CG A:PRO207 4.7 17.5 1.0 NE A:ARG237 4.7 38.5 0.6 N A:ARG237 4.7 18.9 1.0 N A:PRO207 4.9 17.1 1.0 O A:LEU205 4.9 19.2 1.0 CA A:PRO207 5.0 16.5 1.0

C.Sayer, Z.Szabo, M.N.Isupov, C.Ingham, J.A.Littlechild. The Structure of A Novel Thermophilic Esterase From the Planctomycetes Species, Thermogutta Terrifontis Reveals An Open Active Site Due to A Minimal 'Cap' Domain. Front.Microbiol. V. 6 1294 2015.
ISSN: ESSN 1664-302X
PubMed: 26635762
DOI: 10.3389/FMICB.2015.01294