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Chlorine in PDB 3ie5: Crystal Structure of Hyp-1 Protein From Hypericum Perforatum (St John'S Wort) Involved in Hypericin Biosynthesis

Protein crystallography data

The structure of Crystal Structure of Hyp-1 Protein From Hypericum Perforatum (St John'S Wort) Involved in Hypericin Biosynthesis, PDB code: 3ie5 was solved by K.Michalska, H.Fernandes, M.M.Sikorski, M.Jaskolski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.66 / 1.69
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 37.538, 76.713, 119.799, 90.00, 90.00, 90.00
R / Rfree (%) 17 / 20.6

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Hyp-1 Protein From Hypericum Perforatum (St John'S Wort) Involved in Hypericin Biosynthesis (pdb code 3ie5). 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 Hyp-1 Protein From Hypericum Perforatum (St John'S Wort) Involved in Hypericin Biosynthesis, PDB code: 3ie5:

Chlorine binding site 1 out of 1 in 3ie5

Go back to Chlorine Binding Sites List in 3ie5
Chlorine binding site 1 out of 1 in the Crystal Structure of Hyp-1 Protein From Hypericum Perforatum (St John'S Wort) Involved in Hypericin Biosynthesis


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 Hyp-1 Protein From Hypericum Perforatum (St John'S Wort) Involved in Hypericin Biosynthesis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl400

b:38.1
occ:1.00
NZ A:LYS56 3.0 22.1 1.0
O A:HOH193 3.6 48.7 1.0
CE A:LYS56 4.5 25.0 1.0

Reference:

K.Michalska, H.Fernandes, M.M.Sikorski, M.Jaskolski. Crystal Structure of Hyp-1, A St. John'S Wort Protein Implicated in the Biosynthesis of Hypericin J.Struct.Biol. V. 169 161 2010.
ISSN: ISSN 1047-8477
PubMed: 19853038
DOI: 10.1016/J.JSB.2009.10.008
Page generated: Sat Jul 20 21:29:53 2024

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