Zinc in PDB 6wvk: Cryo-Em Structure of Bacillus Subtilis Rna Polymerase in Complex with Held

All present enzymatic activity of Cryo-Em Structure of Bacillus Subtilis Rna Polymerase in Complex with Held:
2.7.7.6; 3.6.4.12;

The structure of Cryo-Em Structure of Bacillus Subtilis Rna Polymerase in Complex with Held 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 in Complex with Held (pdb code 6wvk). 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 in Complex with Held, PDB code: 6wvk:
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 in Complex with Held


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 in Complex with Held within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn2000 b:0.7 occ:1.00 SG D:CYS75 2.2 94.5 1.0 SG D:CYS62 2.3 95.3 1.0 SG D:CYS60 2.3 92.1 1.0 SG D:CYS78 2.4 96.4 1.0 CB D:CYS60 3.3 92.1 1.0 CB D:CYS75 3.3 94.5 1.0 CB D:CYS62 3.4 95.3 1.0 CB D:CYS78 3.5 96.4 1.0 CG1 D:VAL80 4.0 83.7 1.0 O D:LYS64 4.1 92.9 1.0 O D:GLY79 4.3 94.5 1.0 N D:CYS78 4.5 96.4 1.0 CA D:CYS78 4.5 96.4 1.0 O D:CYS75 4.5 94.5 1.0 N D:CYS62 4.6 95.3 1.0 CA D:CYS62 4.6 95.3 1.0 CA D:CYS60 4.6 92.1 1.0 CA D:CYS75 4.6 94.5 1.0 CD1 D:TYR65 4.8 90.6 1.0 CB D:VAL80 4.9 83.7 1.0 C D:CYS75 5.0 94.5 1.0

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


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 in Complex with Held within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn2002 b:42.7 occ:1.00 SG D:CYS902 2.0 27.1 1.0 SG D:CYS818 2.2 34.1 1.0 SG D:CYS899 2.3 28.1 1.0 SG D:CYS892 2.3 31.5 1.0 CB D:CYS902 3.0 27.1 1.0 CB D:CYS818 3.3 34.1 1.0 CB D:CYS892 3.3 31.5 1.0 CB D:CYS899 3.4 28.1 1.0 CA D:CYS892 3.7 31.5 1.0 N D:CYS818 3.9 34.1 1.0 N D:CYS899 4.1 28.1 1.0 NH2 D:ARG887 4.1 28.7 1.0 CA D:CYS902 4.2 27.1 1.0 N D:CYS902 4.2 27.1 1.0 CA D:CYS899 4.2 28.1 1.0 CA D:CYS818 4.2 34.1 1.0 N D:ASN893 4.3 32.8 1.0 OG1 D:THR894 4.4 31.5 1.0 C D:CYS892 4.5 31.5 1.0 OG1 D:THR820 4.5 37.6 1.0 C D:CYS899 4.8 28.1 1.0 O D:CYS899 4.9 28.1 1.0 N D:CYS892 4.9 31.5 1.0 CZ D:ARG887 5.0 28.7 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.