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Magnesium in PDB 8iss: Cryo-Em Structure of Wild-Type Human Trna Splicing Endonuclease Complex Bound to Pre-Trna-Arg at 3.19 A Resolution

Enzymatic activity of Cryo-Em Structure of Wild-Type Human Trna Splicing Endonuclease Complex Bound to Pre-Trna-Arg at 3.19 A Resolution

All present enzymatic activity of Cryo-Em Structure of Wild-Type Human Trna Splicing Endonuclease Complex Bound to Pre-Trna-Arg at 3.19 A Resolution:
4.6.1.16;

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cryo-Em Structure of Wild-Type Human Trna Splicing Endonuclease Complex Bound to Pre-Trna-Arg at 3.19 A Resolution (pdb code 8iss). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Cryo-Em Structure of Wild-Type Human Trna Splicing Endonuclease Complex Bound to Pre-Trna-Arg at 3.19 A Resolution, PDB code: 8iss:

Magnesium binding site 1 out of 1 in 8iss

Go back to Magnesium Binding Sites List in 8iss
Magnesium binding site 1 out of 1 in the Cryo-Em Structure of Wild-Type Human Trna Splicing Endonuclease Complex Bound to Pre-Trna-Arg at 3.19 A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cryo-Em Structure of Wild-Type Human Trna Splicing Endonuclease Complex Bound to Pre-Trna-Arg at 3.19 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg101

b:31.6
occ:1.00
OP2 E:G12 2.1 45.0 1.0
P E:G12 3.4 36.3 1.0
OP2 E:U8 3.5 58.4 1.0
O5' E:G12 3.9 41.9 1.0
OP2 E:G9 4.0 70.7 1.0
C5 E:C13 4.3 37.3 1.0
OP1 E:G12 4.3 31.9 1.0
N7 E:G12 4.4 29.9 1.0
C8 E:G12 4.5 29.8 1.0
O3' E:C11 4.5 41.6 1.0
P E:U8 4.5 66.8 1.0
C3' E:C11 4.6 38.4 1.0
OP1 E:U8 4.6 60.7 1.0
C6 E:C13 4.8 37.0 1.0
O5' E:C11 4.8 53.6 1.0
OP1 E:G9 4.9 73.2 1.0
P E:G9 5.0 73.5 1.0

Reference:

L.Yuan, Y.Han, J.Zhao, Y.Zhang, Y.Sun. Recognition and Cleavage Mechanism of Intron-Containing Pre-Trna By Human Tsen Endonuclease Complex. Nat Commun V. 14 6071 2023.
ISSN: ESSN 2041-1723
PubMed: 37770519
DOI: 10.1038/S41467-023-41845-Y
Page generated: Thu Dec 28 09:29:55 2023

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