Aluminium in PDB 4gnk: Crystal Structure of Galphaq in Complex with Full-Length Human PLCBETA3

All present enzymatic activity of Crystal Structure of Galphaq in Complex with Full-Length Human PLCBETA3:
3.1.4.11;

The structure of Crystal Structure of Galphaq in Complex with Full-Length Human PLCBETA3, PDB code: 4gnk was solved by A.M.Lyon, J.J.G.Tesmer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.99 / 4.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	91.423, 188.845, 293.857, 90.00, 90.00, 90.00
R / Rfree (%)	21.4 / 25.5

The structure of Crystal Structure of Galphaq in Complex with Full-Length Human PLCBETA3 also contains other interesting chemical elements:

Fluorine	(F)	8 atoms
Magnesium	(Mg)	2 atoms
Calcium	(Ca)	2 atoms

The binding sites of Aluminium atom in the Crystal Structure of Galphaq in Complex with Full-Length Human PLCBETA3 (pdb code 4gnk). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total 2 binding sites of Aluminium where determined in the Crystal Structure of Galphaq in Complex with Full-Length Human PLCBETA3, PDB code: 4gnk:
Jump to Aluminium binding site number: 1; 2;

Aluminium binding site 1 out of 2 in the Crystal Structure of Galphaq in Complex with Full-Length Human PLCBETA3


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Crystal Structure of Galphaq in Complex with Full-Length Human PLCBETA3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Al402 b:93.4 occ:1.00 AL A:ALF402 0.0 93.4 1.0 F3 A:ALF402 1.8 93.0 1.0 F2 A:ALF402 1.8 95.0 1.0 F4 A:ALF402 1.8 95.8 1.0 O A:HOH501 1.8 92.1 1.0 F1 A:ALF402 1.9 95.6 1.0 O3B A:GDP401 1.9 94.1 1.0 PB A:GDP401 2.9 94.1 1.0 MG A:MG403 3.1 96.1 1.0 O1B A:GDP401 3.4 94.2 1.0 O A:HOH502 3.6 98.4 1.0 O2B A:GDP401 3.7 93.4 1.0 N A:THR186 3.9 0.8 1.0 O A:HOH503 3.9 96.2 1.0 N A:GLY208 3.9 96.2 1.0 O A:THR186 4.1 95.9 1.0 NH1 A:ARG183 4.2 0.4 1.0 NE2 A:GLN209 4.2 93.7 1.0 O3A A:GDP401 4.2 94.8 1.0 OE1 A:GLN209 4.3 89.9 1.0 NZ A:LYS52 4.4 0.9 1.0 OG1 A:THR186 4.4 0.0 1.0 CB A:THR186 4.5 0.6 1.0 N A:GLU49 4.5 0.3 1.0 CA A:GLY208 4.5 96.4 1.0 CA A:THR186 4.6 0.8 1.0 NH2 A:ARG183 4.6 0.4 1.0 CD A:GLN209 4.6 93.1 1.0 CA A:PRO185 4.7 94.6 1.0 CA A:GLY207 4.7 98.5 1.0 C A:PRO185 4.7 98.9 1.0 C A:THR186 4.7 99.8 1.0 C A:GLY207 4.8 97.1 1.0 CE A:LYS52 4.8 0.8 1.0 CZ A:ARG183 4.9 0.2 1.0 O A:VAL206 5.0 94.5 1.0

Aluminium binding site 2 out of 2 in the Crystal Structure of Galphaq in Complex with Full-Length Human PLCBETA3


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 2 of Crystal Structure of Galphaq in Complex with Full-Length Human PLCBETA3 within 5.0Å range: probe atom residue distance (Å) B Occ C:Al402 b:82.4 occ:1.00 AL C:ALF402 0.0 82.4 1.0 O3B C:GDP401 1.8 87.1 1.0 F3 C:ALF402 1.8 85.3 1.0 F4 C:ALF402 1.8 83.8 1.0 F2 C:ALF402 1.8 85.1 1.0 O C:HOH501 1.8 82.4 1.0 F1 C:ALF402 1.8 82.8 1.0 PB C:GDP401 2.9 87.5 1.0 MG C:MG403 3.3 87.5 1.0 O1B C:GDP401 3.5 86.4 1.0 O2B C:GDP401 3.5 87.0 1.0 O C:HOH502 3.8 85.1 1.0 N C:THR186 4.0 92.7 1.0 O C:HOH503 4.0 89.9 1.0 NH1 C:ARG183 4.0 98.0 1.0 N C:GLY208 4.0 93.1 1.0 OE1 C:GLN209 4.2 92.1 1.0 NE2 C:GLN209 4.2 95.3 1.0 O3A C:GDP401 4.2 86.5 1.0 NZ C:LYS52 4.2 0.2 1.0 O C:THR186 4.3 91.8 1.0 N C:GLU49 4.3 0.7 1.0 NH2 C:ARG183 4.4 98.1 1.0 OG1 C:THR186 4.5 99.5 1.0 CB C:THR186 4.6 96.8 1.0 CA C:GLY208 4.6 94.8 1.0 CD C:GLN209 4.6 94.4 1.0 CA C:PRO185 4.7 90.8 1.0 CZ C:ARG183 4.7 98.0 1.0 CA C:THR186 4.7 94.5 1.0 C C:PRO185 4.8 91.9 1.0 CA C:GLY207 4.8 89.8 1.0 C C:GLY207 4.8 91.0 1.0 CE C:LYS52 4.9 0.9 1.0 CB C:PRO185 4.9 89.9 1.0 C C:THR186 5.0 93.5 1.0

A.M.Lyon, S.Dutta, C.A.Boguth, G.Skiniotis, J.J.Tesmer. Full-Length G Alpha (Q)-Phospholipase C-Beta 3 Structure Reveals Interfaces of the C-Terminal Coiled-Coil Domain. Nat.Struct.Mol.Biol. V. 20 355 2013.
ISSN: ISSN 1545-9993
PubMed: 23377541
DOI: 10.1038/NSMB.2497