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Zinc in PDB 7py7: Cryoem Structure of E.Coli Rna Polymerase Elongation Complex Bound to Nusa and Nusg (Nusa and Nusg Elongation Complex in More-Swiveled Conformation)

Enzymatic activity of Cryoem Structure of E.Coli Rna Polymerase Elongation Complex Bound to Nusa and Nusg (Nusa and Nusg Elongation Complex in More-Swiveled Conformation)

All present enzymatic activity of Cryoem Structure of E.Coli Rna Polymerase Elongation Complex Bound to Nusa and Nusg (Nusa and Nusg Elongation Complex in More-Swiveled Conformation):
2.7.7.6;

Other elements in 7py7:

The structure of Cryoem Structure of E.Coli Rna Polymerase Elongation Complex Bound to Nusa and Nusg (Nusa and Nusg Elongation Complex in More-Swiveled Conformation) also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Cryoem Structure of E.Coli Rna Polymerase Elongation Complex Bound to Nusa and Nusg (Nusa and Nusg Elongation Complex in More-Swiveled Conformation) (pdb code 7py7). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Cryoem Structure of E.Coli Rna Polymerase Elongation Complex Bound to Nusa and Nusg (Nusa and Nusg Elongation Complex in More-Swiveled Conformation), PDB code: 7py7:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 7py7

Go back to Zinc Binding Sites List in 7py7
Zinc binding site 1 out of 2 in the Cryoem Structure of E.Coli Rna Polymerase Elongation Complex Bound to Nusa and Nusg (Nusa and Nusg Elongation Complex in More-Swiveled Conformation)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cryoem Structure of E.Coli Rna Polymerase Elongation Complex Bound to Nusa and Nusg (Nusa and Nusg Elongation Complex in More-Swiveled Conformation) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn1502

b:255.4
occ:1.00
N D:CYS72 2.2 215.5 1.0
CB D:CYS70 2.3 212.0 1.0
SG D:CYS88 2.3 206.2 1.0
CB D:CYS72 2.7 215.5 1.0
CA D:CYS72 2.8 215.5 1.0
N D:LEU71 2.9 200.6 1.0
C D:CYS70 2.9 212.0 1.0
N D:GLY73 3.1 205.2 1.0
CA D:CYS70 3.1 212.0 1.0
C D:LEU71 3.2 200.6 1.0
C D:CYS72 3.4 215.5 1.0
CB D:CYS88 3.5 206.2 1.0
O D:CYS70 3.5 212.0 1.0
CA D:LEU71 3.5 200.6 1.0
SG D:CYS70 3.7 212.0 1.0
O D:LEU71 4.2 200.6 1.0
N D:CYS70 4.3 212.0 1.0
N D:LYS74 4.3 194.6 1.0
CA D:GLY73 4.3 205.2 1.0
CB D:LEU71 4.3 200.6 1.0
SG D:CYS72 4.4 215.5 1.0
CB D:CYS85 4.4 197.8 1.0
SG D:CYS85 4.5 197.8 1.0
O D:CYS72 4.7 215.5 1.0
CA D:CYS88 4.8 206.2 1.0
C D:GLY73 4.9 205.2 1.0

Zinc binding site 2 out of 2 in 7py7

Go back to Zinc Binding Sites List in 7py7
Zinc binding site 2 out of 2 in the Cryoem Structure of E.Coli Rna Polymerase Elongation Complex Bound to Nusa and Nusg (Nusa and Nusg Elongation Complex in More-Swiveled Conformation)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Cryoem Structure of E.Coli Rna Polymerase Elongation Complex Bound to Nusa and Nusg (Nusa and Nusg Elongation Complex in More-Swiveled Conformation) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn1503

b:198.9
occ:1.00
SG D:CYS895 2.3 142.4 1.0
SG D:CYS898 2.3 135.8 1.0
SG D:CYS888 2.3 134.7 1.0
SG D:CYS814 2.3 151.0 1.0
CB D:CYS814 2.9 151.0 1.0
CB D:CYS888 3.1 134.7 1.0
CB D:CYS898 3.4 135.8 1.0
CA D:CYS888 3.6 134.7 1.0
CB D:CYS895 3.7 142.4 1.0
N D:CYS814 3.9 151.0 1.0
NH2 D:ARG883 4.0 142.5 1.0
CA D:CYS814 4.0 151.0 1.0
N D:CYS895 4.2 142.4 1.0
N D:CYS898 4.4 135.8 1.0
CA D:CYS895 4.5 142.4 1.0
CA D:CYS898 4.5 135.8 1.0
N D:ASP889 4.5 144.2 1.0
OG1 D:THR816 4.5 155.4 1.0
C D:CYS888 4.6 134.7 1.0
N D:CYS888 4.6 134.7 1.0
O D:CYS895 4.9 142.4 1.0
C D:CYS895 5.0 142.4 1.0
C D:CYS814 5.0 151.0 1.0
CZ D:ARG883 5.0 142.5 1.0

Reference:

C.Zhu, X.Guo, P.Dumas, M.Takacs, M.Abdelkareem, A.Vanden Broeck, C.Saint-Andre, G.Papai, C.Crucifix, J.Ortiz, A.Weixlbaumer. Transcription Factors Modulate Rna Polymerase Conformational Equilibrium. Nat Commun V. 13 1546 2022.
ISSN: ESSN 2041-1723
PubMed: 35318334
DOI: 10.1038/S41467-022-29148-0
Page generated: Sat Apr 8 01:40:26 2023

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