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PDB 6s08-6sez »
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Sodium in PDB 6s2t: Structure of the N-Terminal Catalytic Region of T. Thermophilus Rel Bound to Ppgpp
Enzymatic activity of Structure of the N-Terminal Catalytic Region of T. Thermophilus Rel Bound to Ppgpp
All present enzymatic activity of Structure of the N-Terminal Catalytic Region of T. Thermophilus Rel Bound to Ppgpp:
2.7.6.5;
2.7.6.5;
Protein crystallography data
The structure of Structure of the N-Terminal Catalytic Region of T. Thermophilus Rel Bound to Ppgpp, PDB code: 6s2t
was solved by
A.Garcia-Pino,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 62.17 / 2.75 |
| Space group | P 41 2 2 |
| Cell size a, b, c (Å), α, β, γ (°) | 87.927, 87.927, 184.252, 90.00, 90.00, 90.00 |
| R / Rfree (%) | 19.6 / 22 |
Other elements in 6s2t:
The structure of Structure of the N-Terminal Catalytic Region of T. Thermophilus Rel Bound to Ppgpp also contains other interesting chemical elements:
| Magnesium | (Mg) | 1 atom |
| Manganese | (Mn) | 1 atom |
| Chlorine | (Cl) | 1 atom |
Sodium Binding Sites:
The binding sites of Sodium atom in the Structure of the N-Terminal Catalytic Region of T. Thermophilus Rel Bound to Ppgpp
(pdb code 6s2t). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Structure of the N-Terminal Catalytic Region of T. Thermophilus Rel Bound to Ppgpp, PDB code: 6s2t:
In total only one binding site of Sodium was determined in the Structure of the N-Terminal Catalytic Region of T. Thermophilus Rel Bound to Ppgpp, PDB code: 6s2t:
Sodium binding site 1 out of 1 in 6s2t
Go back to
Sodium Binding Sites List in 6s2t
Sodium binding site 1 out
of 1 in the Structure of the N-Terminal Catalytic Region of T. Thermophilus Rel Bound to Ppgpp
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Sodium with other atoms in the Na binding
site number 1 of Structure of the N-Terminal Catalytic Region of T. Thermophilus Rel Bound to Ppgpp within 5.0Å range:
|
Reference:
H.Tamman,
K.Van Nerom,
H.Takada,
N.Vandenberk,
D.Scholl,
Y.Polikanov,
J.Hofkens,
A.Talavera,
V.Hauryliuk,
J.Hendrix,
A.Garcia-Pino.
A Nucleotide-Switch Mechanism Mediates Opposing Catalytic Activities of Rel Enzymes. Nat.Chem.Biol. V. 16 834 2020.
ISSN: ESSN 1552-4469
PubMed: 32393900
DOI: 10.1038/S41589-020-0520-2
Page generated: Tue Oct 8 13:22:18 2024
ISSN: ESSN 1552-4469
PubMed: 32393900
DOI: 10.1038/S41589-020-0520-2
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