Zinc in PDB 8pen: Fully Recruited Rfah Bound to E. Coli Transcription Complex Paused at Ops Site (Alternative State of Rfah)

All present enzymatic activity of Fully Recruited Rfah Bound to E. Coli Transcription Complex Paused at Ops Site (Alternative State of Rfah):
2.7.7.6;

The structure of Fully Recruited Rfah Bound to E. Coli Transcription Complex Paused at Ops Site (Alternative State of Rfah) also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Zinc atom in the Fully Recruited Rfah Bound to E. Coli Transcription Complex Paused at Ops Site (Alternative State of Rfah) (pdb code 8pen). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Fully Recruited Rfah Bound to E. Coli Transcription Complex Paused at Ops Site (Alternative State of Rfah), PDB code: 8pen:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Fully Recruited Rfah Bound to E. Coli Transcription Complex Paused at Ops Site (Alternative State of Rfah)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Fully Recruited Rfah Bound to E. Coli Transcription Complex Paused at Ops Site (Alternative State of Rfah) within 5.0Å range: probe atom residue distance (Å) B Occ J:Zn1501 b:195.9 occ:1.00 SG J:CYS85 2.3 162.8 1.0 SG J:CYS88 2.3 159.7 1.0 SG J:CYS70 2.3 158.8 1.0 SG J:CYS72 2.3 157.5 1.0 CB J:CYS85 3.0 157.1 1.0 CB J:CYS72 3.1 152.9 1.0 N J:CYS72 3.7 149.8 1.0 CB J:CYS70 3.8 155.0 1.0 N J:CYS88 3.9 160.0 1.0 CA J:CYS72 3.9 151.0 1.0 CB J:CYS88 4.0 156.4 1.0 CB J:LYS87 4.2 163.1 1.0 CA J:CYS85 4.4 156.6 1.0 N J:GLY73 4.4 151.3 1.0 CA J:CYS88 4.5 156.2 1.0 N J:LEU71 4.6 143.7 1.0 CG1 J:VAL90 4.6 134.4 1.0 C J:CYS72 4.6 151.9 1.0 N J:LYS87 4.6 161.4 1.0 CB J:LYS74 4.7 153.7 1.0 N J:LYS74 4.7 151.7 1.0 CG J:LYS87 4.8 163.7 1.0 C J:LYS87 4.8 163.1 1.0 CA J:LYS87 4.8 162.9 1.0 CA J:CYS70 4.8 152.4 1.0 C J:LEU71 4.8 144.2 1.0 C J:CYS70 4.9 150.2 1.0 C J:CYS85 4.9 157.1 1.0

Zinc binding site 2 out of 2 in the Fully Recruited Rfah Bound to E. Coli Transcription Complex Paused at Ops Site (Alternative State of Rfah)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Fully Recruited Rfah Bound to E. Coli Transcription Complex Paused at Ops Site (Alternative State of Rfah) within 5.0Å range: probe atom residue distance (Å) B Occ J:Zn1502 b:146.7 occ:1.00 SG J:CYS898 2.3 122.7 1.0 SG J:CYS888 2.3 123.5 1.0 SG J:CYS814 2.3 127.0 1.0 SG J:CYS895 2.3 123.4 1.0 CB J:CYS898 2.5 114.1 1.0 CB J:CYS895 3.0 114.8 1.0 NH2 J:ARG883 3.4 121.4 1.0 CB J:CYS888 3.7 116.3 1.0 CA J:CYS898 3.7 109.1 1.0 N J:CYS898 3.8 107.9 1.0 CA J:CYS888 3.9 117.0 1.0 CB J:CYS814 4.0 123.0 1.0 N J:CYS895 4.0 104.7 1.0 CA J:CYS895 4.0 106.6 1.0 N J:CYS814 4.2 120.5 1.0 N J:ASP889 4.4 123.2 1.0 CZ J:ARG883 4.5 117.7 1.0 O J:CYS895 4.5 109.3 1.0 C J:CYS895 4.5 105.7 1.0 NE J:ARG883 4.6 113.8 1.0 C J:CYS888 4.7 120.3 1.0 CA J:CYS814 4.8 124.5 1.0 OG1 J:THR890 4.9 121.2 1.0 OG1 J:THR816 4.9 131.9 1.0 C J:CYS898 4.9 107.3 1.0 N J:CYS888 5.0 116.7 1.0

P.K.Zuber, N.Said, T.Hilal, B.Wang, B.Loll, J.Gonzalez-Higueras, C.A.Ramirez-Sarmiento, G.A.Belogurov, I.Artsimovitch, M.C.Wahl, S.H.Knauer. Concerted Transformation of A Hyper-Paused Transcription Complex and Its Reinforcing Protein. Nat Commun V. 15 3040 2024.
ISSN: ESSN 2041-1723
PubMed: 38589445
DOI: 10.1038/S41467-024-47368-4