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Zinc in PDB 7mli: Crystal Structure of Thermus Thermophilus Reiterative Transcription Complex with 5NT Oligo-C Rna

Enzymatic activity of Crystal Structure of Thermus Thermophilus Reiterative Transcription Complex with 5NT Oligo-C Rna

All present enzymatic activity of Crystal Structure of Thermus Thermophilus Reiterative Transcription Complex with 5NT Oligo-C Rna:
2.7.7.6;

Protein crystallography data

The structure of Crystal Structure of Thermus Thermophilus Reiterative Transcription Complex with 5NT Oligo-C Rna, PDB code: 7mli was solved by Y.Liu, R.H.Ebright, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.96 / 3.60
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 187.076, 103.883, 298.739, 90, 97.95, 90
R / Rfree (%) 24.3 / 29.2

Other elements in 7mli:

The structure of Crystal Structure of Thermus Thermophilus Reiterative Transcription Complex with 5NT Oligo-C Rna also contains other interesting chemical elements:

Magnesium (Mg) 5 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Thermus Thermophilus Reiterative Transcription Complex with 5NT Oligo-C Rna (pdb code 7mli). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Thermus Thermophilus Reiterative Transcription Complex with 5NT Oligo-C Rna, PDB code: 7mli:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 7mli

Go back to Zinc Binding Sites List in 7mli
Zinc binding site 1 out of 2 in the Crystal Structure of Thermus Thermophilus Reiterative Transcription Complex with 5NT Oligo-C Rna


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Thermus Thermophilus Reiterative Transcription Complex with 5NT Oligo-C Rna within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn2001

b:110.0
occ:1.00
SG D:CYS1201 2.3 96.3 1.0
SG D:CYS1194 2.3 122.4 1.0
SG D:CYS1112 2.3 111.3 1.0
SG D:CYS1204 2.3 79.5 1.0
CB D:CYS1204 3.0 134.6 1.0
CB D:CYS1194 3.2 91.7 1.0
CB D:CYS1112 3.5 120.8 1.0
CA D:CYS1194 3.6 83.5 1.0
CB D:CYS1201 3.7 96.0 1.0
OG1 D:THR1196 3.8 122.1 1.0
N D:GLN1195 4.0 113.2 1.0
N D:CYS1112 4.1 137.7 1.0
CA D:CYS1204 4.2 111.6 1.0
N D:CYS1204 4.2 105.7 1.0
N D:CYS1201 4.2 139.8 1.0
C D:CYS1194 4.3 93.4 1.0
NH2 D:ARG1189 4.3 106.8 1.0
CG2 D:THR1114 4.4 129.5 1.0
CA D:CYS1112 4.4 118.0 1.0
CA D:CYS1201 4.5 128.4 1.0
N D:THR1196 4.7 101.3 1.0
N D:CYS1194 4.8 79.9 1.0
CB D:THR1196 4.9 141.5 1.0

Zinc binding site 2 out of 2 in 7mli

Go back to Zinc Binding Sites List in 7mli
Zinc binding site 2 out of 2 in the Crystal Structure of Thermus Thermophilus Reiterative Transcription Complex with 5NT Oligo-C Rna


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Thermus Thermophilus Reiterative Transcription Complex with 5NT Oligo-C Rna within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn2002

b:179.2
occ:1.00
SG D:CYS76 2.3 195.6 1.0
SG D:CYS60 2.3 183.5 1.0
SG D:CYS73 2.3 196.5 1.0
SG D:CYS58 2.3 185.0 1.0
CB D:CYS73 3.1 149.9 1.0
CB D:CYS58 3.1 190.8 1.0
CB D:CYS76 3.4 164.2 1.0
N D:CYS60 3.7 178.5 1.0
CB D:CYS60 3.7 161.3 1.0
N D:CYS76 3.9 172.3 1.0
N D:LYS62 4.0 193.2 1.0
N D:GLY61 4.0 189.3 1.0
CB D:LYS62 4.1 188.5 1.0
CA D:CYS60 4.1 186.7 1.0
N D:ALA59 4.2 170.2 1.0
CA D:CYS76 4.3 177.4 1.0
CA D:CYS58 4.4 167.7 1.0
C D:CYS60 4.4 198.7 1.0
C D:CYS58 4.4 150.4 1.0
CA D:CYS73 4.5 147.5 1.0
CA D:LYS62 4.6 195.0 1.0
C D:ALA59 4.7 160.5 1.0
CB D:ARG75 4.8 116.4 1.0
CD1 D:TYR63 4.8 185.3 1.0
CA D:ALA59 4.9 166.1 1.0
C D:GLY61 4.9 200.1 1.0
CA D:GLY61 5.0 184.2 1.0
N D:TYR63 5.0 188.4 1.0
C D:ARG75 5.0 160.5 1.0

Reference:

Y.Liu, L.Yu, C.Pukhrambam, J.T.Winkelman, E.Firlar, J.T.Kaelber, Y.Zhang, B.E.Nickels, R.H.Ebright. Structural and Mechanistic Basis of Reiterative Transcription Initiation. Proc.Natl.Acad.Sci.Usa V. 119 2022.
ISSN: ESSN 1091-6490
PubMed: 35082149
DOI: 10.1073/PNAS.2115746119
Page generated: Sat Apr 8 00:35:18 2023

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