4QJ3: PDB entry 4QJ3

Structure of a fragment of human phospholipase C-beta3 delta472-559, in complex with Galphaq. Determined by X-ray diffraction at 3.0 Å resolution. Released 22 Oct 2014.

Method: X-ray diffraction
Resolution: 3.0 Å
Organisms: Mus musculus, Homo sapiens
Chains: 2
Atoms: 8,747
Mol. weight: 135.62 kDa
Ligands: CA, MG, ALF, GDP
Released: 22 Oct 2014

Explore 4QJ3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4QJ3 contains 63 α-helices and 46 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 20 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	39-45	7	1
α-helix	52-62	11
α-helix	69-73	5
α-helix	76-96	21
α-helix	106-114	9
α-helix	118-120	3
α-helix	128-136	9
α-helix	139-146	8
α-helix	148-150	3
α-helix	157-161	5
α-helix	164-168	5
α-helix	176-181	6
β-strand	189-195	7	1
β-strand	200-206	7	1
α-helix	210-214	5
α-helix	216-219	4
β-strand	225-231	7	1
α-helix	232-236	5
β-strand	238	1	2
β-strand	246	1	2
α-helix	247-258	12
α-helix	262-264	3
β-strand	268-274	7	1
α-helix	276-282	7
α-helix	288-290	3
α-helix	302-314	13
β-strand	324-328	5	1
α-helix	334-351	18

Chain B: 43 helices, 38 β-strands

Element	Residues	Length	Sheet
α-helix	20-24	5
β-strand	26-31	6	3
β-strand	38-45	8	3
β-strand	51-55	5	3
α-helix	60	1
β-strand	61-65	5	3
α-helix	66-68	3
β-strand	69-74	6	3
α-helix	79-80	2
α-helix	84-90	7
α-helix	97-101	5
β-strand	103-108	6	3
β-strand	116-122	7	3
α-helix	128-139	12
α-helix	142-145	4
α-helix	149-162	14
β-strand	170-171	2	4
α-helix	172-178	7
α-helix	183-192	10
β-strand	202-203	2	4
α-helix	205-207	3
α-helix	210-220	11
α-helix	224-232	9
β-strand	242	1	5
α-helix	243-252	10
α-helix	265-268	4
α-helix	269-279	11
α-helix	283-287	5
β-strand	290	1	5
α-helix	293-300	8
α-helix	310-313	4
α-helix	323-325	3
β-strand	326-331	6	6
β-strand	336	1	7
β-strand	342-343	2	8
β-strand	345	1	7
α-helix	348-355	8
β-strand	360-363	4	6
β-strand	365-366	2	9
α-helix	367-369	3
β-strand	376-377	2	9
β-strand	383-384	2	8
β-strand	387-388	2	9
α-helix	389-399	11
β-strand	408-412	5	6
α-helix	419-433	15
α-helix	434-436	3
β-strand	437	1	6
α-helix	451-455	5
β-strand	463-466	4	6
α-helix	588-591	4
β-strand	598-599	2	6
α-helix	605-611	7
β-strand	616-621	6	6
α-helix	622-631	10
α-helix	633-642	10
β-strand	644-648	5	6
α-helix	662-665	4
β-strand	671-674	4	6
α-helix	681-689	9
β-strand	698-700	3	6
α-helix	701-702	2
α-helix	703-705	3
α-helix	719-720	2
β-strand	726-736	11	10
β-strand	745-752	8	10
β-strand	759	1	10
β-strand	763	1	10
α-helix	764-767	4
β-strand	775	1	10
β-strand	781-786	6	10
α-helix	789-791	3
β-strand	793-800	8	10
β-strand	805-812	8	10
α-helix	816-818	3
β-strand	819-826	8	10
α-helix	831	1
β-strand	832-846	15	10
α-helix	853-860	8
α-helix	862-875	14
α-helix	877-880	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Guanine nucleotide-binding protein G(q) subunit alpha	A	protein	379	Mus musculus	P21279 (AlphaFold model)
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3	B	protein	793	Homo sapiens	Q01970 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4QJ3_1 Guanine nucleotide-binding protein G(q) subunit alpha (chains A)
MSYYHHHHHHDYDIPTTENLYFQGAAMACCLSEEAKEARRINDEIERQLRRDKRDARREL
KLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVYQNIFTAMQAMIRAMDTLKIP
YKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYY
LNDLDRVADPSYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCF
ENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLE
EKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFV
FAAVKDTILQLNLKEYNLV

Sequence of entity 2 (B), FASTA

>4QJ3_2 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 (chains B)
MAHHHHHHGTALQLEPPTVVETLRRGSKFIKWDEETSSRNLVTLRVDPNGFFLYWTGPNM
EVDTLDISSIRDTRTGRYARLPKDPKIREVLGFGGPDARLEEKLMTVVSGPDPVNTVFLN
FMAVQDDTAKVWSEELFKLAMNILAQNASRNTFLRKAYTKLKLQVNQDGRIPVKNILKMF
SADKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIGAKGKP
YLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRY
LGGEENGILPLEALDLSTDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCR
CVELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEAIAETAFKTSPYPVILSFENHVDSA
KQQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKRPKKPTTDEG
TASSEVNATEEMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVE
YNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGY
LLKPEFMRRPDKSFDPFTEVIVDGIVANALRVKVISGQFLSDRKVGIYVEVDMFGLPVDT
RRKYRTRTSQGNSFNPVWDEEPFDFPKVVLPTLASLRIAAFEEGGKFVGHRILPVSAIRS
GYHYVCLRNEANQPLCLPALLIYTEASDYIPDDHQDYAEALINPIKHVSLMDQRARQLAA
LIGESEAQAGQET

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	1
MG	Magnesium ion	Mg	1
ALF	Tetrafluoroaluminate ion	Al F4	1
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	1

Primary citation

Molecular mechanisms of phospholipase C beta 3 autoinhibition. Lyon, A.M., Begley, J.A., Manett, T.D. et al. Structure (2014) 22:1844-1854. DOI 10.1016/j.str.2014.10.008 · PubMed

Other PDB entries of the same protein (UniProt P21279 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5DO9 2.6 Å, Structure of regulator of G protein signaling 8 (RGS8) in complex with AlF4-activated…
7SQ2 2.6 Å, Reprocessed and refined structure of Phospholipase C-beta and Gq signaling complex
4EKD 2.71 Å, Structure of human regulator of G protein signaling 2 (RGS2) in complex with murine…
8YFS 2.8 Å, MRGPRE-Gq-scFv16-complex
3AH8 2.9 Å, Structure of heterotrimeric G protein Galpha-q beta gamma in complex with an inhibitor…
2BCJ 3.06 Å, Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-q and…
4QJ4 3.3 Å, Structure of a fragment of human phospholipase C-beta3 delta472-569, bound to IP3 and in…
4QJ5 3.41 Å, Structure of a fragment of human phospholipase C-beta3 delta472-581, bound to IP3 and in…
2RGN 3.5 Å, Crystal Structure of p63RhoGEF complex with Galpha-q and RhoA
4GNK 4.0 Å, Crystal structure of Galphaq in complex with full-length human PLCbeta3
4EKC 7.4 Å, Structure of human regulator of G protein signaling 2 (RGS2) in complex with murine…

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