Chlorine in PDB 6eqf: Crystal Structure of A Polyethylene Terephthalate Degrading Hydrolase From Ideonella Sakaiensis in Spacegroup P212121

Enzymatic activity of Crystal Structure of A Polyethylene Terephthalate Degrading Hydrolase From Ideonella Sakaiensis in Spacegroup P212121

All present enzymatic activity of Crystal Structure of A Polyethylene Terephthalate Degrading Hydrolase From Ideonella Sakaiensis in Spacegroup P212121:
3.1.1.101;

Protein crystallography data

The structure of Crystal Structure of A Polyethylene Terephthalate Degrading Hydrolase From Ideonella Sakaiensis in Spacegroup P212121, PDB code: 6eqf was solved by H.P.Austin, M.D.Allen, C.W.Johnson, G.T.Beckham, J.E.Mcgeehan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.73 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 51.349, 64.130, 68.240, 90.00, 90.00, 90.00
R / Rfree (%) 14.9 / 18.6

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of A Polyethylene Terephthalate Degrading Hydrolase From Ideonella Sakaiensis in Spacegroup P212121 (pdb code 6eqf). 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 A Polyethylene Terephthalate Degrading Hydrolase From Ideonella Sakaiensis in Spacegroup P212121, PDB code: 6eqf:

Chlorine binding site 1 out of 1 in 6eqf

Go back to Chlorine Binding Sites List in 6eqf
Chlorine binding site 1 out of 1 in the Crystal Structure of A Polyethylene Terephthalate Degrading Hydrolase From Ideonella Sakaiensis in Spacegroup P212121


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 A Polyethylene Terephthalate Degrading Hydrolase From Ideonella Sakaiensis in Spacegroup P212121 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl301

b:13.3
occ:1.00
OG A:SER160 2.9 12.9 1.0
O A:HOH547 3.1 16.3 1.0
N A:TYR87 3.3 7.9 1.0
N A:MET161 3.3 9.9 1.0
CB A:SER160 3.4 13.2 1.0
CG A:MET161 3.4 8.8 1.0
CB A:TYR87 3.5 13.3 1.0
CB A:MET161 3.7 11.7 1.0
CA A:TYR87 4.0 10.4 1.0
CA A:MET161 4.1 5.6 1.0
O A:HOH596 4.1 32.0 1.0
SD A:MET161 4.1 13.5 1.0
CA A:GLY86 4.2 9.5 1.0
C A:GLY86 4.2 11.5 1.0
C A:SER160 4.3 8.7 1.0
CA A:SER160 4.4 7.9 1.0
CE A:MET161 4.4 15.8 1.0
O A:HOH447 4.5 26.1 1.0
CG A:TYR87 4.7 11.5 1.0
NE2 A:HIS237 4.9 12.3 1.0
O A:TYR87 4.9 12.1 1.0

Reference:

H.P.Austin, M.D.Allen, B.S.Donohoe, N.A.Rorrer, F.L.Kearns, R.L.Silveira, B.C.Pollard, G.Dominick, R.Duman, K.El Omari, V.Mykhaylyk, A.Wagner, W.E.Michener, A.Amore, M.S.Skaf, M.F.Crowley, A.W.Thorne, C.W.Johnson, H.L.Woodcock, J.E.Mcgeehan, G.T.Beckham. Characterization and Engineering of A Plastic-Degrading Aromatic Polyesterase. Proc. Natl. Acad. Sci. V. 115 E4350 2018U.S.A..
ISSN: ESSN 1091-6490
PubMed: 29666242
DOI: 10.1073/PNAS.1718804115
Page generated: Sat Dec 12 12:56:03 2020

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