Zinc in PDB 8hsr: Thermus Thermophilus Rho-Engaged Rnap Elongation Complex

All present enzymatic activity of Thermus Thermophilus Rho-Engaged Rnap Elongation Complex:
2.7.7.6;

The structure of Thermus Thermophilus Rho-Engaged Rnap Elongation Complex also contains other interesting chemical elements:

Magnesium	(Mg)	7 atoms
Fluorine	(F)	18 atoms

The binding sites of Zinc atom in the Thermus Thermophilus Rho-Engaged Rnap Elongation Complex (pdb code 8hsr). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Thermus Thermophilus Rho-Engaged Rnap Elongation Complex, PDB code: 8hsr:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Thermus Thermophilus Rho-Engaged Rnap Elongation Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Thermus Thermophilus Rho-Engaged Rnap Elongation Complex within 5.0Å range: probe atom residue distance (Å) B Occ J:Zn1601 b:445.4 occ:1.00 CB J:CYS76 1.7 409.4 1.0 SG J:CYS58 2.3 375.9 1.0 SG J:CYS60 2.3 419.4 1.0 SG J:CYS73 2.3 414.6 1.0 SG J:CYS76 2.3 409.4 1.0 CA J:CYS76 3.1 409.4 1.0 CB J:CYS58 3.4 375.9 1.0 CB J:CYS73 3.4 414.6 1.0 N J:GLY61 3.6 405.7 1.0 N J:CYS76 3.7 409.4 1.0 N J:CYS60 3.8 419.4 1.0 CB J:CYS60 3.9 419.4 1.0 C J:CYS76 4.0 409.4 1.0 CA J:CYS60 4.2 419.4 1.0 C J:ARG75 4.3 418.9 1.0 N J:GLY77 4.3 371.4 1.0 N J:ALA59 4.4 404.4 1.0 C J:CYS60 4.4 419.4 1.0 CA J:GLY61 4.4 405.7 1.0 N J:LYS62 4.6 405.5 1.0 CA J:CYS58 4.6 375.9 1.0 O J:ARG75 4.6 418.9 1.0 C J:CYS58 4.7 375.9 1.0 O J:CYS76 4.7 409.4 1.0 CA J:CYS73 4.8 414.6 1.0 C J:ALA59 4.9 404.4 1.0

Zinc binding site 2 out of 2 in the Thermus Thermophilus Rho-Engaged Rnap Elongation Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Thermus Thermophilus Rho-Engaged Rnap Elongation Complex within 5.0Å range: probe atom residue distance (Å) B Occ J:Zn1602 b:129.3 occ:1.00 SG J:CYS1201 2.3 102.0 1.0 SG J:CYS1112 2.3 111.3 1.0 SG J:CYS1204 2.3 97.9 1.0 SG J:CYS1194 2.3 96.2 1.0 CB J:CYS1204 2.7 97.9 1.0 CB J:CYS1194 3.2 96.2 1.0 CB J:CYS1201 3.3 102.0 1.0 CA J:CYS1194 3.4 96.2 1.0 CB J:CYS1112 3.6 111.3 1.0 OG1 J:THR1114 3.8 102.6 1.0 N J:CYS1201 3.9 102.0 1.0 CA J:CYS1204 3.9 97.9 1.0 N J:GLN1195 4.0 95.8 1.0 N J:CYS1204 4.1 97.9 1.0 NH2 J:ARG1189 4.2 89.0 1.0 CA J:CYS1201 4.2 102.0 1.0 C J:CYS1194 4.3 96.2 1.0 N J:CYS1112 4.4 111.3 1.0 OG1 J:THR1196 4.4 102.4 1.0 CA J:CYS1112 4.5 111.3 1.0 N J:CYS1194 4.6 96.2 1.0 CB J:THR1114 4.6 102.6 1.0 O J:CYS1112 4.7 111.3 1.0 NE J:ARG1189 4.7 89.0 1.0 C J:CYS1201 4.9 102.0 1.0 CZ J:ARG1189 4.9 89.0 1.0 O J:CYS1201 4.9 102.0 1.0 N J:THR1196 5.0 102.4 1.0 C J:CYS1112 5.0 111.3 1.0

Y.Murayama, H.Ehara, M.Aoki, M.Goto, T.Yokoyama, S.I.Sekine. Structural Basis of the Transcription Termination Factor Rho Engagement with Transcribing Rna Polymerase From Thermus Thermophilus. Sci Adv V. 9 E7093 2023.
ISSN: ESSN 2375-2548
PubMed: 36753546
DOI: 10.1126/SCIADV.ADE7093