Zinc in PDB 1exj: Crystal Structure of Transcription Activator Bmrr, From B. Subtilis, Bound to 21 Base Pair Bmr Operator and Tpp

The structure of Crystal Structure of Transcription Activator Bmrr, From B. Subtilis, Bound to 21 Base Pair Bmr Operator and Tpp, PDB code: 1exj was solved by E.E.Zheleznova-Heldwein, R.G.Brennan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	16.00 / 3.00
Space group	P 43 2 2
Cell size a, b, c (Å), α, β, γ (°)	109.490, 109.490, 144.320, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The structure of Crystal Structure of Transcription Activator Bmrr, From B. Subtilis, Bound to 21 Base Pair Bmr Operator and Tpp also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Zinc atom in the Crystal Structure of Transcription Activator Bmrr, From B. Subtilis, Bound to 21 Base Pair Bmr Operator and Tpp (pdb code 1exj). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Transcription Activator Bmrr, From B. Subtilis, Bound to 21 Base Pair Bmr Operator and Tpp, PDB code: 1exj:

Zinc binding site 1 out of 1 in the Crystal Structure of Transcription Activator Bmrr, From B. Subtilis, Bound to 21 Base Pair Bmr Operator and Tpp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Transcription Activator Bmrr, From B. Subtilis, Bound to 21 Base Pair Bmr Operator and Tpp within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:18.3 occ:0.50 NE2 A:HIS189 2.4 41.8 1.0 CE1 A:HIS189 3.2 41.3 1.0 CD2 A:HIS189 3.5 41.1 1.0 ND1 A:HIS189 4.4 41.4 1.0 CG A:HIS189 4.6 37.5 1.0 NE A:ARG188 4.8 65.2 1.0 CG A:ARG188 4.9 32.1 1.0 CB A:GLU138 5.0 35.3 1.0

E.E.Heldwein, R.G.Brennan. Crystal Structure of the Transcription Activator Bmrr Bound to Dna and A Drug. Nature V. 409 378 2001.
ISSN: ISSN 0028-0836
PubMed: 11201751
DOI: 10.1038/35053138