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

Enzymatic activity of The Structure of A Novel Thermophilic Esterase From the Planctomycetes Species, Thermogutta Terrifontis, EST2-Butyrate Bound

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

Protein crystallography data

The structure of The Structure of A Novel Thermophilic Esterase From the Planctomycetes Species, Thermogutta Terrifontis, EST2-Butyrate Bound, PDB code: 5aob 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) 51.55 / 1.79
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 61.684, 70.578, 75.305, 90.00, 90.00, 90.00
R / Rfree (%) 17.6 / 22.1

Chlorine Binding Sites:

The binding sites of Chlorine atom in the The Structure of A Novel Thermophilic Esterase From the Planctomycetes Species, Thermogutta Terrifontis, EST2-Butyrate Bound (pdb code 5aob). 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 The Structure of A Novel Thermophilic Esterase From the Planctomycetes Species, Thermogutta Terrifontis, EST2-Butyrate Bound, PDB code: 5aob:

Chlorine binding site 1 out of 1 in 5aob

Go back to Chlorine Binding Sites List in 5aob
Chlorine binding site 1 out of 1 in the The Structure of A Novel Thermophilic Esterase From the Planctomycetes Species, Thermogutta Terrifontis, EST2-Butyrate Bound


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-Butyrate Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1290

b:36.5
occ:0.70
 O A:HOH2148 2.7 39.0 1.0
N A:ASN217 2.9 30.6 1.0
O A:HOH2147 2.9 44.9 1.0
N A:HIS248 3.1 26.4 1.0
CB A:HIS248 3.6 30.4 1.0
CB A:ALA247 3.7 27.8 1.0
O A:ALA215 3.7 32.1 1.0
CB A:ASN217 3.7 43.6 1.0
CA A:ASP216 3.7 25.8 1.0
CA A:ASN217 3.8 33.3 1.0
C A:ASP216 3.8 24.9 1.0
CA A:ALA247 3.9 26.3 1.0
ND2 A:ASN217 3.9 65.9 1.0
OD1 A:ASP216 4.0 22.6 1.0
CA A:HIS248 4.0 30.6 1.0
C A:ALA247 4.0 26.1 1.0
N A:THR218 4.1 29.7 1.0
CG A:ASN217 4.1 52.8 1.0
O A:HOH2170 4.3 47.2 1.0
C A:ASN217 4.3 36.2 1.0
O A:HOH2144 4.3 47.6 1.0
CG A:ASP216 4.5 31.9 1.0
OG1 A:THR218 4.5 31.5 1.0
C A:ALA215 4.6 34.9 1.0
N A:ASP216 4.7 29.7 1.0
CB A:ASP216 4.7 27.7 1.0
O A:HIS248 4.9 28.1 1.0
CG A:HIS248 4.9 28.1 1.0
C A:HIS248 5.0 29.2 1.0
O A:ASP216 5.0 27.5 1.0

Reference:

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
Page generated: Fri Jul 26 05:23:01 2024

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