Aluminium in PDB 4qj3: Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq

Enzymatic activity of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq

All present enzymatic activity of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq:
3.1.4.11;

Protein crystallography data

The structure of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq, PDB code: 4qj3 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)*	29.71 / 3.00
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	200.623, 88.761, 92.232, 90.00, 101.39, 90.00
*R / R_free (%)*	19.5 / 24

Other elements in 4qj3:

The structure of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq also contains other interesting chemical elements:

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

Aluminium Binding Sites:

The binding sites of Aluminium atom in the Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq (pdb code 4qj3). 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 Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq, PDB code: 4qj3:

Aluminium binding site 1 out of 1 in 4qj3

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Aluminium Binding Sites List in 4qj3

Aluminium binding site 1 out of 1 in the Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq

Mono view

Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Al401 b:30.6 occ:1.00	AL	A:ALF401	0.0	30.6	1.0
	F1	A:ALF401	1.8	30.8	1.0
	F4	A:ALF401	1.8	30.1	1.0
	F3	A:ALF401	1.8	30.9	1.0
	F2	A:ALF401	1.8	31.2	1.0
	O3B	A:GDP400	1.9	30.0	1.0
	O	A:HOH501	1.9	18.1	1.0
	PB	A:GDP400	3.1	29.9	1.0
	MG	A:MG402	3.3	32.8	1.0
	O2B	A:GDP400	3.7	30.9	1.0
	NH1	A:ARG183	3.8	36.5	1.0
	N	A:GLU49	3.9	33.6	1.0
	NH2	A:ARG183	3.9	37.0	1.0
	N	A:GLY208	4.0	36.7	1.0
	O1B	A:GDP400	4.0	29.9	1.0
	O	A:HOH508	4.0	16.3	1.0
	N	A:THR186	4.0	37.2	1.0
	OE1	A:GLN209	4.1	36.4	1.0
	NZ	A:LYS52	4.1	33.3	1.0
	NE2	A:GLN209	4.1	35.1	1.0
	OG1	A:THR186	4.2	36.1	1.0
	CB	A:THR186	4.3	37.4	1.0
	O3A	A:GDP400	4.3	29.4	1.0
	CA	A:GLY48	4.3	34.8	1.0
	CZ	A:ARG183	4.3	36.4	1.0
	CE	A:LYS52	4.4	34.0	1.0
	O	A:THR186	4.5	38.8	1.0
	CD	A:GLN209	4.5	36.1	1.0
	CA	A:GLY207	4.6	38.0	1.0
	C	A:GLY48	4.6	33.9	1.0
	CA	A:THR186	4.7	37.9	1.0
	CA	A:GLY208	4.8	36.8	1.0
	CA	A:GLU49	4.8	33.3	1.0
	C	A:GLY207	4.8	37.7	1.0
	O	A:VAL206	4.9	37.7	1.0
	CA	A:PRO185	4.9	37.2	1.0
	O2A	A:GDP400	5.0	30.1	1.0
	C	A:PRO185	5.0	37.8	1.0

Reference:

A.M.Lyon, J.A.Begley, T.Manett, J.J.G.Tesmer. Molecular Mechanisms of Plcbeta Regulation. Structure 2014.
ISSN: ISSN 0969-2126

Page generated: Sat Dec 12 01:33:28 2020

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