Zinc in PDB 6wvj: Cryo-Em Structure of Bacillus Subtilis Rna Polymerase Elongation Complex

All present enzymatic activity of Cryo-Em Structure of Bacillus Subtilis Rna Polymerase Elongation Complex:
2.7.7.6;

The structure of Cryo-Em Structure of Bacillus Subtilis Rna Polymerase Elongation Complex also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Zinc atom in the Cryo-Em Structure of Bacillus Subtilis Rna Polymerase Elongation Complex (pdb code 6wvj). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Cryo-Em Structure of Bacillus Subtilis Rna Polymerase Elongation Complex, PDB code: 6wvj:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Cryo-Em Structure of Bacillus Subtilis Rna Polymerase Elongation Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cryo-Em Structure of Bacillus Subtilis Rna Polymerase Elongation Complex within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn2000 b:0.4 occ:1.00 SG D:CYS62 2.1 0.2 1.0 SG D:CYS75 2.2 90.5 1.0 SG D:CYS60 2.3 93.0 1.0 SG D:CYS78 2.4 94.9 1.0 CB D:CYS62 3.0 0.2 1.0 O D:CYS60 3.2 93.0 1.0 CB D:CYS75 3.3 90.5 1.0 CB D:CYS78 3.4 94.9 1.0 N D:CYS62 3.5 0.2 1.0 CB D:CYS60 3.5 93.0 1.0 CA D:CYS62 3.6 0.2 1.0 C D:CYS62 3.9 0.2 1.0 CB D:LYS64 4.0 92.5 1.0 C D:CYS60 4.0 93.0 1.0 N D:LYS64 4.1 92.5 1.0 O D:CYS62 4.2 0.2 1.0 N D:CYS78 4.3 94.9 1.0 CA D:CYS60 4.4 93.0 1.0 N D:GLY63 4.4 97.5 1.0 CA D:CYS78 4.5 94.9 1.0 NH2 D:ARG77 4.5 97.9 1.0 CA D:LYS64 4.6 92.5 1.0 C D:HIS61 4.6 96.0 1.0 N D:TYR65 4.7 89.9 1.0 CA D:CYS75 4.7 90.5 1.0 N D:HIS61 4.9 96.0 1.0

Zinc binding site 2 out of 2 in the Cryo-Em Structure of Bacillus Subtilis Rna Polymerase Elongation Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Cryo-Em Structure of Bacillus Subtilis Rna Polymerase Elongation Complex within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn2002 b:82.5 occ:1.00 SG D:CYS902 2.1 56.2 1.0 SG D:CYS899 2.2 57.6 1.0 SG D:CYS818 2.3 67.9 1.0 SG D:CYS892 2.3 60.2 1.0 CB D:CYS902 3.1 56.2 1.0 CB D:CYS899 3.2 57.6 1.0 CB D:CYS818 3.3 67.9 1.0 CB D:CYS892 3.4 60.2 1.0 CA D:CYS892 3.7 60.2 1.0 N D:CYS818 4.0 67.9 1.0 N D:CYS899 4.1 57.6 1.0 N D:CYS902 4.1 56.2 1.0 CA D:CYS899 4.1 57.6 1.0 CA D:CYS902 4.2 56.2 1.0 NH2 D:ARG887 4.3 55.3 1.0 CA D:CYS818 4.3 67.9 1.0 OG1 D:THR820 4.3 68.8 1.0 N D:ASN893 4.4 60.4 1.0 O D:CYS899 4.4 57.6 1.0 C D:CYS892 4.5 60.2 1.0 C D:CYS899 4.6 57.6 1.0 OG1 D:THR894 4.6 58.1 1.0 N D:CYS892 4.8 60.2 1.0 CB D:THR820 4.8 68.8 1.0 OD2 D:ASP817 4.9 61.8 1.0

T.P.Newing, A.J.Oakley, M.Miller, C.Dawson, S.Brown, J.Bouwer, G.Tolun, P.J.Lewis. Transcription Complex Recycling By the Atpase Motor Protein Held To Be Published.