Zinc in PDB 8pfj: Fully Recruited Rfah Bound to E. Coli Transcription Complex Paused at Ops Site (Not Fully Complementary Scaffold; Alternative State of Rfah)

Enzymatic activity of Fully Recruited Rfah Bound to E. Coli Transcription Complex Paused at Ops Site (Not Fully Complementary Scaffold; Alternative State of Rfah)

All present enzymatic activity of Fully Recruited Rfah Bound to E. Coli Transcription Complex Paused at Ops Site (Not Fully Complementary Scaffold; Alternative State of Rfah):
2.7.7.6;

Other elements in 8pfj:

The structure of Fully Recruited Rfah Bound to E. Coli Transcription Complex Paused at Ops Site (Not Fully Complementary Scaffold; Alternative State of Rfah) also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Fully Recruited Rfah Bound to E. Coli Transcription Complex Paused at Ops Site (Not Fully Complementary Scaffold; Alternative State of Rfah) (pdb code 8pfj). 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 (Not Fully Complementary Scaffold; Alternative State of Rfah), PDB code: 8pfj:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 8pfj

Go back to Zinc Binding Sites List in 8pfj
Zinc binding site 1 out of 2 in the Fully Recruited Rfah Bound to E. Coli Transcription Complex Paused at Ops Site (Not Fully Complementary Scaffold; 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 (Not Fully Complementary Scaffold; Alternative State of Rfah) within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Zn1501

b:201.9
occ:1.00
 SG J:CYS85 2.3 163.6 1.0
SG J:CYS70 2.3 166.7 1.0
SG J:CYS88 2.3 159.2 1.0
SG J:CYS72 2.3 168.5 1.0
CB J:CYS72 3.0 163.7 1.0
CB J:CYS85 3.1 158.5 1.0
N J:CYS72 3.6 160.8 1.0
CB J:CYS70 3.8 161.8 1.0
CA J:CYS72 3.8 162.1 1.0
N J:CYS88 4.0 162.6 1.0
CB J:CYS88 4.0 157.9 1.0
CB J:LYS87 4.3 168.4 1.0
N J:GLY73 4.3 159.7 1.0
CG1 J:VAL90 4.4 140.4 1.0
C J:CYS72 4.5 162.1 1.0
CA J:CYS85 4.5 156.8 1.0
N J:LYS74 4.6 155.9 1.0
N J:LEU71 4.6 157.2 1.0
CA J:CYS88 4.6 159.1 1.0
CB J:LYS74 4.7 154.8 1.0
C J:LEU71 4.8 158.5 1.0
N J:LYS87 4.8 166.9 1.0
NZ J:LYS87 4.8 169.1 1.0
C J:LYS87 4.9 168.4 1.0
C J:CYS85 4.9 159.1 1.0
CA J:LYS87 4.9 168.3 1.0
CA J:CYS70 4.9 160.0 1.0
C J:CYS70 4.9 160.7 1.0
CG J:LYS87 5.0 169.2 1.0

Zinc binding site 2 out of 2 in 8pfj

Go back to Zinc Binding Sites List in 8pfj
Zinc binding site 2 out of 2 in the Fully Recruited Rfah Bound to E. Coli Transcription Complex Paused at Ops Site (Not Fully Complementary Scaffold; 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 (Not Fully Complementary Scaffold; Alternative State of Rfah) within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Zn1502

b:151.0
occ:1.00
 SG J:CYS888 2.3 134.6 1.0
SG J:CYS814 2.3 131.0 1.0
SG J:CYS898 2.3 130.3 1.0
SG J:CYS895 2.3 128.6 1.0
CB J:CYS898 2.7 121.5 1.0
CB J:CYS895 3.2 122.4 1.0
CB J:CYS888 3.5 125.6 1.0
CA J:CYS888 3.7 124.0 1.0
NH2 J:ARG883 3.8 125.6 1.0
CA J:CYS898 3.9 117.3 1.0
N J:CYS898 3.9 115.5 1.0
CB J:CYS814 4.0 129.5 1.0
N J:CYS895 4.0 117.3 1.0
CA J:CYS895 4.1 118.7 1.0
N J:CYS814 4.3 127.1 1.0
N J:ASP889 4.4 126.5 1.0
O J:CYS895 4.6 117.9 1.0
C J:CYS888 4.6 126.9 1.0
C J:CYS895 4.6 117.1 1.0
OG1 J:THR890 4.6 133.0 1.0
CA J:CYS814 4.8 129.0 1.0
CZ J:ARG883 4.8 122.5 1.0
N J:CYS888 4.8 122.8 1.0
NE J:ARG883 4.8 119.8 1.0

Reference:

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
Page generated: Thu Oct 31 09:28:06 2024

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