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Chlorine in PDB 3vw1: Crystal Strucuture of the Crystal Violet-Bound Form of Ramr (Transcriptional Regurator of Tetr Family) From Salmonella Typhimurium

Protein crystallography data

The structure of Crystal Strucuture of the Crystal Violet-Bound Form of Ramr (Transcriptional Regurator of Tetr Family) From Salmonella Typhimurium, PDB code: 3vw1 was solved by K.Sakurai, S.Yamasaki, R.Nakashima, E.Nikaido, A.Yamaguchi, K.Nishino, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 22.28 / 2.21
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 43.594, 54.741, 92.711, 104.45, 97.25, 89.93
R / Rfree (%) 22 / 25.4

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Strucuture of the Crystal Violet-Bound Form of Ramr (Transcriptional Regurator of Tetr Family) From Salmonella Typhimurium (pdb code 3vw1). 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 Strucuture of the Crystal Violet-Bound Form of Ramr (Transcriptional Regurator of Tetr Family) From Salmonella Typhimurium, PDB code: 3vw1:

Chlorine binding site 1 out of 1 in 3vw1

Go back to Chlorine Binding Sites List in 3vw1
Chlorine binding site 1 out of 1 in the Crystal Strucuture of the Crystal Violet-Bound Form of Ramr (Transcriptional Regurator of Tetr Family) From Salmonella Typhimurium


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Strucuture of the Crystal Violet-Bound Form of Ramr (Transcriptional Regurator of Tetr Family) From Salmonella Typhimurium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl202

b:43.4
occ:1.00
NH1 A:ARG35 3.2 39.2 1.0
NH2 A:ARG35 3.3 35.6 1.0
CZ A:ARG35 3.7 45.6 1.0

Reference:

S.Yamasaki, E.Nikaido, R.Nakashima, K.Sakurai, D.Fujiwara, I.Fujii, K.Nishino. The Crystal Structure of Multidrug-Resistance Regulator Ramr with Multiple Drugs Nat Commun V. 4 2078 2013.
ISSN: ESSN 2041-1723
PubMed: 23800819
DOI: 10.1038/NCOMMS3078
Page generated: Sun Jul 21 07:13:33 2024

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