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Aluminium in PDB 7jl0: Cryo-Em Structure of MDA5-Dsrna in Complex with TRIM65 Pspry Domain (Monomer)

Enzymatic activity of Cryo-Em Structure of MDA5-Dsrna in Complex with TRIM65 Pspry Domain (Monomer)

All present enzymatic activity of Cryo-Em Structure of MDA5-Dsrna in Complex with TRIM65 Pspry Domain (Monomer):
3.6.4.13;

Other elements in 7jl0:

The structure of Cryo-Em Structure of MDA5-Dsrna in Complex with TRIM65 Pspry Domain (Monomer) also contains other interesting chemical elements:

Fluorine (F) 4 atoms
Magnesium (Mg) 1 atom
Zinc (Zn) 1 atom

Aluminium Binding Sites:

The binding sites of Aluminium atom in the Cryo-Em Structure of MDA5-Dsrna in Complex with TRIM65 Pspry Domain (Monomer) (pdb code 7jl0). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total only one binding site of Aluminium was determined in the Cryo-Em Structure of MDA5-Dsrna in Complex with TRIM65 Pspry Domain (Monomer), PDB code: 7jl0:

Aluminium binding site 1 out of 1 in 7jl0

Go back to Aluminium Binding Sites List in 7jl0
Aluminium binding site 1 out of 1 in the Cryo-Em Structure of MDA5-Dsrna in Complex with TRIM65 Pspry Domain (Monomer)


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Cryo-Em Structure of MDA5-Dsrna in Complex with TRIM65 Pspry Domain (Monomer) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al1103

b:43.8
occ:1.00
AL A:ALF1103 0.0 43.8 1.0
F2 A:ALF1103 1.8 43.8 1.0
F3 A:ALF1103 1.8 43.8 1.0
F1 A:ALF1103 1.8 43.8 1.0
F4 A:ALF1103 1.8 43.8 1.0
O2B A:ADP1102 2.4 48.0 1.0
O1B A:ADP1102 2.4 48.0 1.0
PB A:ADP1102 2.6 48.0 1.0
MG A:MG1104 2.9 24.6 1.0
O3B A:ADP1102 3.1 48.0 1.0
NH2 A:ARG822 3.9 48.5 1.0
O3A A:ADP1102 4.1 48.0 1.0
CE A:LYS335 4.5 48.5 1.0
NH1 A:ARG822 4.5 48.5 1.0
NZ A:LYS335 4.6 48.5 1.0
CZ A:ARG822 4.7 48.5 1.0
NE2 A:GLN818 4.7 48.5 1.0
OE2 A:GLU444 5.0 48.5 1.0

Reference:

K.Kato, S.Ahmad, Z.Zhu, J.M.Young, X.Mu, S.Park, H.S.Malik, S.Hur. Structural Analysis of Rig-I-Like Receptors Reveals Ancient Rules of Engagement Between Diverse Rna Helicases and Trim Ubiquitin Ligases Mol.Cell 2020.
ISSN: ISSN 1097-2765
Page generated: Wed Jul 10 09:58:53 2024

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