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Calcium in PDB 4qj5: Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-581, Bound to IP3 and in Complex with Galphaq

Enzymatic activity of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-581, Bound to IP3 and in Complex with Galphaq

All present enzymatic activity of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-581, 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 DELTA472-581, Bound to IP3 and in Complex with Galphaq, PDB code: 4qj5 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) 29.34 / 3.41
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 205.918, 89.869, 93.261, 90.00, 101.80, 90.00
R / Rfree (%) 21.2 / 27.7

Other elements in 4qj5:

The structure of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-581, 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 DELTA472-581, Bound to IP3 and in Complex with Galphaq (pdb code 4qj5). 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 DELTA472-581, Bound to IP3 and in Complex with Galphaq, PDB code: 4qj5:

Calcium binding site 1 out of 1 in 4qj5

Go back to Calcium Binding Sites List in 4qj5
Calcium binding site 1 out of 1 in the Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-581, 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 DELTA472-581, Bound to IP3 and in Complex with Galphaq within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca901

b:0.9
occ:1.00
OD2 B:ASP364 2.3 1.0 1.0
OD1 B:ASN333 2.3 0.6 1.0
OE1 B:GLU413 2.3 0.6 1.0
OE2 B:GLU362 2.3 0.5 1.0
OD1 B:ASP364 2.3 0.1 1.0
O11 B:I3P902 2.5 0.1 1.0
CG B:ASP364 2.6 0.0 1.0
CD B:GLU362 3.1 0.3 1.0
O2 B:I3P902 3.1 0.5 1.0
CD B:GLU413 3.4 0.9 1.0
CG B:ASN333 3.4 0.9 1.0
OE1 B:GLU362 3.7 0.0 1.0
P1 B:I3P902 3.8 0.3 1.0
CG B:GLU362 3.8 99.3 1.0
ND2 B:ASN333 3.9 0.8 1.0
OE2 B:GLU413 4.0 0.6 1.0
CB B:ASP364 4.1 0.6 1.0
O1 B:I3P902 4.2 0.1 1.0
CB B:GLU413 4.4 0.1 1.0
OH B:TYR335 4.4 0.3 1.0
O13 B:I3P902 4.4 0.9 1.0
C2 B:I3P902 4.4 1.0 1.0
CG B:GLU413 4.5 0.6 1.0
CB B:ASN333 4.7 0.8 1.0
CA B:ASN333 4.8 99.6 1.0
CB B:GLU362 4.9 97.6 1.0
CE1 B:TYR335 4.9 0.7 1.0
CA B:ASP364 4.9 0.7 1.0
O43 B:I3P902 4.9 0.1 1.0
NE2 B:HIS332 4.9 99.7 1.0
O12 B:I3P902 5.0 0.6 1.0
C1 B:I3P902 5.0 0.5 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: Sun Jul 14 12:26:42 2024

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