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Chlorine in PDB 5w8e: The Structure of A Coa-Dependent Acyl-Homoserine Lactone Synthase, Bjai, with the Adduct of Sah and IV-Coa

Protein crystallography data

The structure of The Structure of A Coa-Dependent Acyl-Homoserine Lactone Synthase, Bjai, with the Adduct of Sah and IV-Coa, PDB code: 5w8e was solved by S.-H.Dong, S.K.Nair, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 1.80
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 91.270, 91.270, 98.120, 90.00, 90.00, 120.00
R / Rfree (%) 19.6 / 21.7

Chlorine Binding Sites:

The binding sites of Chlorine atom in the The Structure of A Coa-Dependent Acyl-Homoserine Lactone Synthase, Bjai, with the Adduct of Sah and IV-Coa (pdb code 5w8e). 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 Coa-Dependent Acyl-Homoserine Lactone Synthase, Bjai, with the Adduct of Sah and IV-Coa, PDB code: 5w8e:

Chlorine binding site 1 out of 1 in 5w8e

Go back to Chlorine Binding Sites List in 5w8e
Chlorine binding site 1 out of 1 in the The Structure of A Coa-Dependent Acyl-Homoserine Lactone Synthase, Bjai, with the Adduct of Sah and IV-Coa


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 Coa-Dependent Acyl-Homoserine Lactone Synthase, Bjai, with the Adduct of Sah and IV-Coa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl302

b:27.3
occ:1.00
NH2 A:ARG43 3.4 25.5 1.0
NH1 A:ARG43 3.4 24.4 1.0
CZ A:ARG43 3.8 24.9 1.0
CG1 A:VAL45 4.3 28.6 1.0
O A:HOH477 4.6 35.4 1.0
O A:HOH570 4.6 33.8 1.0
CG2 A:VAL45 4.7 29.2 1.0
CB A:VAL45 4.9 28.0 1.0

Reference:

S.H.Dong, N.D.Frane, Q.H.Christensen, E.P.Greenberg, R.Nagarajan, S.K.Nair. Molecular Basis For the Substrate Specificity of Quorum Signal Synthases. Proc. Natl. Acad. Sci. V. 114 9092 2017U.S.A..
ISSN: ESSN 1091-6490
PubMed: 28784791
DOI: 10.1073/PNAS.1705400114
Page generated: Fri Jul 26 19:15:44 2024

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