Calcium in PDB 4qj4: Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-569, Bound to IP3 and in Complex with Galphaq

Enzymatic activity of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-569, Bound to IP3 and in Complex with Galphaq

All present enzymatic activity of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-569, Bound to IP3 and in Complex with Galphaq:
3.1.4.11;

Protein crystallography data

The structure of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-569, Bound to IP3 and in Complex with Galphaq, PDB code: 4qj4 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)*	29.40 / 3.30
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	201.923, 89.191, 92.639, 90.00, 101.70, 90.00
*R / R_free (%)*	20.8 / 26.7

Other elements in 4qj4:

The structure of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-569, Bound to IP3 and in Complex with Galphaq also contains other interesting chemical elements:

Fluorine	(F)	4 atoms
Magnesium	(Mg)	1 atom
Aluminium	(Al)	1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-569, Bound to IP3 and in Complex with Galphaq (pdb code 4qj4). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-569, Bound to IP3 and in Complex with Galphaq, PDB code: 4qj4:

Calcium binding site 1 out of 1 in 4qj4

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Calcium Binding Sites List in 4qj4

Calcium binding site 1 out of 1 in the Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-569, Bound to IP3 and in Complex with Galphaq

Mono view

Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-569, Bound to IP3 and in Complex with Galphaq within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Ca901 b:84.0 occ:1.00	O2	B:I3P902	2.3	0.4	1.0
	OD1	B:ASN333	2.3	80.9	1.0
	OD2	B:ASP364	2.3	87.2	1.0
	OE2	B:GLU362	2.3	83.4	1.0
	OE1	B:GLU413	2.3	89.3	1.0
	OD1	B:ASP364	2.3	84.6	1.0
	CG	B:ASP364	2.6	86.3	1.0
	O11	B:I3P902	2.9	0.2	1.0
	CD	B:GLU362	3.1	80.7	1.0
	CG	B:ASN333	3.2	81.7	1.0
	CD	B:GLU413	3.6	91.8	1.0
	ND2	B:ASN333	3.6	83.7	1.0
	OE1	B:GLU362	3.6	79.3	1.0
	C2	B:I3P902	3.7	0.8	1.0
	CG	B:GLU362	4.0	79.6	1.0
	O1	B:I3P902	4.1	0.6	1.0
	P1	B:I3P902	4.1	0.8	1.0
	CB	B:ASP364	4.2	88.0	1.0
	OE2	B:GLU413	4.3	93.6	1.0
	OH	B:TYR335	4.4	91.7	1.0
	O3	B:I3P902	4.4	0.0	1.0
	CB	B:GLU413	4.5	90.0	1.0
	C1	B:I3P902	4.5	0.6	1.0
	CB	B:ASN333	4.5	80.4	1.0
	CG	B:GLU413	4.6	91.9	1.0
	C3	B:I3P902	4.6	0.2	1.0
	NE2	B:HIS332	4.6	83.1	1.0
	CA	B:ASN333	4.7	79.7	1.0
	N	B:ASN333	4.8	78.3	1.0
	O13	B:I3P902	4.9	0.3	1.0
	CE1	B:TYR335	4.9	89.6	1.0
	CD2	B:HIS332	4.9	81.2	1.0
	CA	B:ASP364	4.9	87.8	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: Wed Jul 9 01:44:22 2025

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