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Zinc in PDB 8t0l: E. Coli SW2/SNF2 Atpase Rapa Bound to Both Adp-ALF3 and Reconstituted E. Coli Rna Polymerase Post-Termination Complex on Negatively- Supercoiled Dna

Enzymatic activity of E. Coli SW2/SNF2 Atpase Rapa Bound to Both Adp-ALF3 and Reconstituted E. Coli Rna Polymerase Post-Termination Complex on Negatively- Supercoiled Dna

All present enzymatic activity of E. Coli SW2/SNF2 Atpase Rapa Bound to Both Adp-ALF3 and Reconstituted E. Coli Rna Polymerase Post-Termination Complex on Negatively- Supercoiled Dna:
2.7.7.6;

Other elements in 8t0l:

The structure of E. Coli SW2/SNF2 Atpase Rapa Bound to Both Adp-ALF3 and Reconstituted E. Coli Rna Polymerase Post-Termination Complex on Negatively- Supercoiled Dna also contains other interesting chemical elements:

Fluorine (F) 3 atoms
Magnesium (Mg) 1 atom
Aluminium (Al) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the E. Coli SW2/SNF2 Atpase Rapa Bound to Both Adp-ALF3 and Reconstituted E. Coli Rna Polymerase Post-Termination Complex on Negatively- Supercoiled Dna (pdb code 8t0l). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the E. Coli SW2/SNF2 Atpase Rapa Bound to Both Adp-ALF3 and Reconstituted E. Coli Rna Polymerase Post-Termination Complex on Negatively- Supercoiled Dna, PDB code: 8t0l:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 8t0l

Go back to Zinc Binding Sites List in 8t0l
Zinc binding site 1 out of 2 in the E. Coli SW2/SNF2 Atpase Rapa Bound to Both Adp-ALF3 and Reconstituted E. Coli Rna Polymerase Post-Termination Complex on Negatively- Supercoiled Dna


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of E. Coli SW2/SNF2 Atpase Rapa Bound to Both Adp-ALF3 and Reconstituted E. Coli Rna Polymerase Post-Termination Complex on Negatively- Supercoiled Dna within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Zn1402

b:308.7
occ:1.00
CB J:CYS70 2.0 199.8 1.0
CB J:CYS85 2.1 186.1 1.0
SG J:CYS72 2.3 190.3 1.0
SG J:CYS85 2.3 186.1 1.0
SG J:CYS88 2.3 185.2 1.0
SG J:CYS70 2.3 199.8 1.0
CA J:CYS70 3.4 199.8 1.0
CA J:CYS85 3.6 186.1 1.0
CG2 J:VAL90 3.7 187.5 1.0
C J:CYS70 3.9 199.8 1.0
CB J:CYS72 4.0 190.3 1.0
CB J:CYS88 4.1 185.2 1.0
N J:CYS72 4.2 190.3 1.0
N J:LEU71 4.2 185.0 1.0
N J:CYS85 4.3 186.1 1.0
N J:CYS70 4.5 199.8 1.0
C J:CYS85 4.5 186.1 1.0
N J:CYS88 4.5 185.2 1.0
CA J:CYS72 4.6 190.3 1.0
O J:CYS70 4.6 199.8 1.0
O J:VAL90 4.6 187.5 1.0
N J:GLY73 4.7 192.5 1.0
CB J:LYS74 4.7 200.3 1.0
N J:LYS74 4.7 200.3 1.0
CA J:CYS88 4.8 185.2 1.0
O J:CYS85 4.8 186.1 1.0

Zinc binding site 2 out of 2 in 8t0l

Go back to Zinc Binding Sites List in 8t0l
Zinc binding site 2 out of 2 in the E. Coli SW2/SNF2 Atpase Rapa Bound to Both Adp-ALF3 and Reconstituted E. Coli Rna Polymerase Post-Termination Complex on Negatively- Supercoiled Dna


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of E. Coli SW2/SNF2 Atpase Rapa Bound to Both Adp-ALF3 and Reconstituted E. Coli Rna Polymerase Post-Termination Complex on Negatively- Supercoiled Dna within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Zn1403

b:151.1
occ:1.00
CB J:CYS898 1.8 92.2 1.0
SG J:CYS888 2.2 105.5 1.0
SG J:CYS895 2.2 92.5 1.0
SG J:CYS898 2.3 92.2 1.0
SG J:CYS814 2.3 109.4 1.0
CB J:CYS895 3.0 92.5 1.0
NH2 J:ARG883 3.0 101.5 1.0
CB J:CYS888 3.0 105.5 1.0
CA J:CYS898 3.2 92.2 1.0
CZ J:ARG883 3.7 101.5 1.0
N J:CYS898 3.7 92.2 1.0
NE J:ARG883 3.9 101.5 1.0
CA J:CYS888 3.9 105.5 1.0
CB J:CYS814 4.1 109.4 1.0
CA J:CYS895 4.2 92.5 1.0
OG1 J:THR816 4.2 115.4 1.0
N J:CYS895 4.2 92.5 1.0
C J:CYS898 4.3 92.2 1.0
O J:CYS898 4.7 92.2 1.0
NH1 J:ARG883 4.7 101.5 1.0
N J:CYS814 4.7 109.4 1.0
O J:CYS895 4.7 92.5 1.0
C J:CYS895 4.8 92.5 1.0
C J:CYS888 4.8 105.5 1.0
O J:SER884 4.9 96.6 1.0
N J:CYS888 4.9 105.5 1.0
N J:ASP889 4.9 114.7 1.0

Reference:

J.J.Brewer, K.Inlow, R.A.Mooney, B.Bosch, P.D.B.Olinares, L.P.Marcelino, B.T.Chait, R.Landick, J.Gelles, E.A.Campbell, S.A.Darst. Rapa Opens the Rna Polymerase Clamp to Disrupt Post-Termination Complexes and Prevent Cytotoxic R-Loop Formation. Nat.Struct.Mol.Biol. 2025.
ISSN: ESSN 1545-9985
PubMed: 39779919
DOI: 10.1038/S41594-024-01447-8
Page generated: Fri Aug 22 13:35:40 2025

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