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

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

All present enzymatic activity of The Structure of A Novel Thermophilic Esterase From the Planctomycetes Species, Thermogutta Terrifontis, EST2-Valerate 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-Valerate Bound, PDB code: 5aoc 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) 51.81 / 1.79
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 61.991, 70.874, 75.932, 90.00, 90.00, 90.00
R / Rfree (%) 18.5 / 24.1

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-Valerate Bound (pdb code 5aoc). 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-Valerate Bound, PDB code: 5aoc:

Chlorine binding site 1 out of 1 in 5aoc

Go back to Chlorine Binding Sites List in 5aoc
Chlorine binding site 1 out of 1 in the The Structure of A Novel Thermophilic Esterase From the Planctomycetes Species, Thermogutta Terrifontis, EST2-Valerate 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-Valerate Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1296

b:34.9
occ:0.70
 O A:HOH2167 2.6 44.1 1.0
O A:HOH2165 2.9 41.9 1.0
N A:HIS248 3.1 25.2 1.0
N A:ASN217 3.1 27.7 1.0
CB A:HIS248 3.4 26.0 1.0
CB A:ALA247 3.7 28.7 1.0
CA A:ASP216 3.9 29.0 1.0
CA A:HIS248 3.9 24.8 1.0
CA A:ALA247 3.9 26.0 1.0
O A:HOH2189 3.9 50.0 1.0
O A:ALA215 3.9 31.7 1.0
OD1 A:ASP216 3.9 27.6 1.0
C A:ASP216 4.0 25.2 1.0
CA A:ASN217 4.0 41.0 1.0
CB A:ASN217 4.0 42.4 1.0
C A:ALA247 4.0 25.2 1.0
N A:THR218 4.1 31.1 1.0
ND2 A:ASN217 4.2 63.3 1.0
OG1 A:THR218 4.2 36.1 1.0
CG A:ASN217 4.4 49.4 1.0
C A:ASN217 4.4 37.3 1.0
CG A:ASP216 4.5 27.7 1.0
O A:HOH2163 4.6 46.9 1.0
O A:HIS248 4.7 23.2 1.0
CG A:HIS248 4.8 25.9 1.0
CB A:ASP216 4.8 26.7 1.0
C A:ALA215 4.8 28.0 1.0
N A:ASP216 4.8 25.3 1.0
C A:HIS248 4.8 26.6 1.0
CB A:THR218 4.9 30.4 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: Sat Dec 12 11:31:13 2020

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