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Aluminium in PDB 8uqn: PLCB3-Gaq Complex on Membranes

Enzymatic activity of PLCB3-Gaq Complex on Membranes

All present enzymatic activity of PLCB3-Gaq Complex on Membranes:
3.1.4.11;

Other elements in 8uqn:

The structure of PLCB3-Gaq Complex on Membranes also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Calcium (Ca) 1 atom
Fluorine (F) 4 atoms

Aluminium Binding Sites:

The binding sites of Aluminium atom in the PLCB3-Gaq Complex on Membranes (pdb code 8uqn). 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 PLCB3-Gaq Complex on Membranes, PDB code: 8uqn:

Aluminium binding site 1 out of 1 in 8uqn

Go back to Aluminium Binding Sites List in 8uqn
Aluminium binding site 1 out of 1 in the PLCB3-Gaq Complex on Membranes


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of PLCB3-Gaq Complex on Membranes within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al402

b:72.8
occ:1.00
AL A:ALF402 0.0 72.8 1.0
F1 A:ALF402 1.8 72.8 1.0
F3 A:ALF402 1.8 72.8 1.0
F4 A:ALF402 1.8 72.8 1.0
F2 A:ALF402 1.8 72.8 1.0
O A:HOH501 2.3 20.0 1.0
O3B A:GDP401 2.3 67.3 1.0
O2B A:GDP401 2.6 67.3 1.0
H2 A:HOH501 2.6 20.0 1.0
PB A:GDP401 2.9 67.3 1.0
H1 A:HOH501 3.2 20.0 1.0
O1B A:GDP401 3.5 67.3 1.0
OE1 A:GLN209 4.0 70.5 1.0
NH1 A:ARG183 4.1 67.5 1.0
N A:THR186 4.1 66.4 1.0
N A:GLY208 4.1 65.5 1.0
OG1 A:THR186 4.1 66.4 1.0
N A:GLU49 4.3 73.2 1.0
O3A A:GDP401 4.4 67.3 1.0
CB A:THR186 4.4 66.4 1.0
MG A:MG403 4.4 67.9 1.0
O A:THR186 4.5 66.4 1.0
NE2 A:GLN209 4.6 70.5 1.0
NH2 A:ARG183 4.6 67.5 1.0
CA A:GLY208 4.7 65.5 1.0
C A:GLY207 4.7 63.4 1.0
CA A:GLY48 4.7 72.1 1.0
CD A:GLN209 4.7 70.5 1.0
CA A:THR186 4.7 66.4 1.0
CA A:GLY207 4.8 63.4 1.0
CE A:LYS52 4.8 62.7 1.0
CZ A:ARG183 4.8 67.5 1.0
NZ A:LYS52 4.9 62.7 1.0
CA A:PRO185 4.9 67.9 1.0
C A:PRO185 5.0 67.9 1.0

Reference:

M.E.Falzone, R.Mackinnon. The Mechanism of G Alpha Q Regulation of Plc Beta 3 -Catalyzed PIP2 Hydrolysis. Proc.Natl.Acad.Sci.Usa V. 120 11120 2023.
ISSN: ESSN 1091-6490
PubMed: 37991948
DOI: 10.1073/PNAS.2315011120
Page generated: Wed Jul 10 10:45:20 2024

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