4GNK: Galphaq

Crystal structure of Galphaq in complex with full-length human PLCbeta3. Determined by X-ray diffraction at 4.0 Å resolution. Released 6 Feb 2013.

Method: X-ray diffraction
Resolution: 4.0 Å
Organisms: Mus musculus, Homo sapiens
Chains: 5
Atoms: 19,764
Mol. weight: 393.28 kDa
Ligands: CA, MG, ALF, GDP
Released: 6 Feb 2013

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

Secondary structure: helices and β-sheets

4GNK contains 138 α-helices and 102 β-strands across 5 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
α-helix	20-36	17
β-strand	39-46	8	1
α-helix	53-63	11
α-helix	69-72	4
α-helix	76-96	21
α-helix	99-101	3
α-helix	106-114	9
α-helix	126-136	11
α-helix	139-146	8
α-helix	157-162	6
α-helix	164-168	5
α-helix	176-181	6
β-strand	189-196	8	1
β-strand	199-206	8	1
α-helix	210-216	7
α-helix	217-219	3
β-strand	225-231	7	1
α-helix	232-234	3
β-strand	238	1	2
β-strand	246	1	2
α-helix	247-260	14
β-strand	268-274	7	1
α-helix	276-283	8
α-helix	288-291	4
α-helix	298	1
α-helix	303-314	12
β-strand	325-328	4	1
α-helix	334-352	19

Chain B: 43 helices, 44 β-strands

Element	Residues	Length	Sheet
α-helix	20-24	5
β-strand	27-32	6	3
β-strand	37-42	6	3
β-strand	44-45	2	4
β-strand	51-55	5	4
β-strand	61-65	5	4
α-helix	66-68	3
β-strand	69-74	6	3
α-helix	75-77	3
α-helix	84-90	7
β-strand	103-108	6	3
β-strand	116-122	7	3
α-helix	127-139	13
α-helix	142-145	4
α-helix	149-162	14
β-strand	170-171	2	5
α-helix	172-178	7
α-helix	184-193	10
β-strand	202-203	2	5
α-helix	210-220	11
α-helix	224-232	9
β-strand	240-242	3	6
α-helix	243-249	7
α-helix	250-254	5
α-helix	265-268	4
α-helix	269-279	11
α-helix	283-286	4
β-strand	290-292	3	6
α-helix	293-300	8
α-helix	310-313	4
α-helix	323-325	3
β-strand	326-328	3	7
β-strand	330	1	8
β-strand	331	1	9
β-strand	336	1	10
β-strand	345	1	10
α-helix	348-356	9
β-strand	360-363	4	8
β-strand	365-366	2	11
β-strand	376-377	2	11
β-strand	387-388	2	11
α-helix	389-399	11
β-strand	408-412	5	8
α-helix	419-432	14
α-helix	434-436	3
β-strand	437	1	8
β-strand	449	1	12
α-helix	451-455	5
α-helix	457-459	3
β-strand	463-465	3	8
β-strand	574	1	13
β-strand	578	1	13
α-helix	583-586	4
α-helix	590-592	3
β-strand	598-599	2	7
α-helix	605-610	6
β-strand	613	1	12
β-strand	616-621	6	7
α-helix	622-631	10
α-helix	633-640	8
β-strand	644-648	5	7
α-helix	662-665	4
β-strand	671-672	2	7
β-strand	674	1	9
α-helix	681-689	9
β-strand	698-700	3	7
α-helix	701-702	2
α-helix	703-706	4
α-helix	719-720	2
β-strand	726-736	11	14
β-strand	745-752	8	14
β-strand	759	1	14
β-strand	763	1	14
α-helix	764-767	4
β-strand	775	1	14
β-strand	781-786	6	14
β-strand	793-800	8	14
α-helix	801-803	3
β-strand	805-812	8	14
α-helix	816-818	3
β-strand	819-826	8	14
α-helix	831	1
β-strand	832-846	15	14
α-helix	850-852	3
α-helix	853-860	8
α-helix	862-875	14
α-helix	877-880	4

Chain C: 21 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	39-46	8	15
α-helix	52-63	12
α-helix	69-72	4
α-helix	76-96	21
α-helix	99-101	3
α-helix	105-114	10
α-helix	126-136	11
α-helix	139-146	8
α-helix	157-162	6
α-helix	164-168	5
α-helix	176-181	6
β-strand	189-195	7	15
β-strand	200-206	7	15
α-helix	210-216	7
α-helix	217-219	3
β-strand	225-231	7	15
α-helix	232-234	3
α-helix	237	1
β-strand	238	1	16
α-helix	239	1
β-strand	246	1	16
α-helix	247-260	14
α-helix	262-264	3
β-strand	268-274	7	15
α-helix	276-283	8
α-helix	288-291	4
α-helix	304-315	12
β-strand	325-328	4	15
α-helix	334-352	19

Chain D: 44 helices, 42 β-strands

Element	Residues	Length	Sheet
α-helix	20-24	5
β-strand	27-32	6	3
β-strand	37-42	6	3
β-strand	44-45	2	17
β-strand	51-55	5	17
β-strand	61-65	5	17
α-helix	66-68	3
β-strand	69-74	6	3
α-helix	75-77	3
α-helix	84-90	7
β-strand	103-108	6	3
β-strand	116-122	7	3
α-helix	127-139	13
α-helix	142-145	4
α-helix	149-162	14
β-strand	170-171	2	18
α-helix	172-178	7
α-helix	184-193	10
β-strand	202-203	2	18
α-helix	210-220	11
α-helix	224-232	9
β-strand	240-242	3	19
α-helix	243-249	7
α-helix	250-254	5
α-helix	265-268	4
α-helix	269-279	11
α-helix	283-286	4
β-strand	290-292	3	19
α-helix	293-300	8
α-helix	310-313	4
α-helix	323-325	3
β-strand	326-328	3	20
β-strand	330	1	21
β-strand	331	1	22
β-strand	336	1	23
β-strand	345	1	23
α-helix	347-356	10
β-strand	360-363	4	21
β-strand	365-366	2	24
β-strand	376-377	2	24
β-strand	387-388	2	24
α-helix	389-399	11
β-strand	408-412	5	21
α-helix	419-432	14
α-helix	434-436	3
β-strand	437	1	21
β-strand	449	1	25
α-helix	451-455	5
α-helix	457-459	3
β-strand	463-465	3	21
α-helix	578-580	3
α-helix	583-586	4
α-helix	590-592	3
β-strand	598-599	2	20
α-helix	605-610	6
β-strand	613	1	25
β-strand	616-621	6	20
α-helix	622-631	10
α-helix	633-640	8
β-strand	644-648	5	20
α-helix	662-665	4
β-strand	671-672	2	20
β-strand	674	1	22
α-helix	681-689	9
β-strand	698-700	3	20
α-helix	701-702	2
α-helix	703-706	4
α-helix	719-720	2
β-strand	726-736	11	26
β-strand	745-752	8	26
β-strand	759	1	26
β-strand	763	1	26
α-helix	764-767	4
β-strand	775	1	26
β-strand	781-786	6	26
β-strand	793-800	8	26
α-helix	801-803	3
β-strand	805-812	8	26
α-helix	816-818	3
β-strand	819-826	8	26
α-helix	831	1
β-strand	832-846	15	26
α-helix	850-852	3
α-helix	853-860	8
α-helix	862-875	14
α-helix	877-880	4

Chain E: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	935-937	3
α-helix	938-945	8
α-helix	947-949	3
α-helix	954-959	6
α-helix	961-1007	47
α-helix	1028-1086	59
α-helix	1090-1104	15
α-helix	1121-1144	24
α-helix	1146-1182	37
α-helix	1187-1189	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Guanine nucleotide-binding protein G(q) subunit alpha	A, C	protein	353	Mus musculus	P21279 (AlphaFold model)
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3	B, D	protein	1235	Homo sapiens	Q01970 (AlphaFold model)
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3	E	protein	259	Homo sapiens	Q01970 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>4GNK_1 Guanine nucleotide-binding protein G(q) subunit alpha (chains A, C)
MACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSG
YSDEDKRGFTKLVYQNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFEN
PYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPSYLPTQQDVLRVRVPT
TGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNEN
RMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAR
EFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV

Sequence of entity 2 (B, D), FASTA

>4GNK_2 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 (chains B, D)
MAHHHHHHGTALQLEPPTVVETLRRGSKFIKWDEETSSRNLVTLRVDPNGFFLYWTGPNM
EVDTLDISSIRDTRTGRYARLPKDPKIREVLGFGGPDARLEEKLMTVVSGPDPVNTVFLN
FMAVQDDTAKVWSEELFKLAMNILAQNASRNTFLRKAYTKLKLQVNQDGRIPVKNILKMF
SADKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIGAKGKP
YLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRY
LGGEENGILPLEALDLSTDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCR
CVELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEAIAETAFKTSPYPVILSFENHVDSA
KQQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKRHRPSAGGPD
SAGRKRPLEQSNSALSESSAATEPSSPQLGSPSSDSCPGLSNGEEVGLEKPSLEPQKSLG
DEGLNRGPYVLGPADREDEEEDEEEEEQTDPKKPTTDEGTASSEVNATEEMSTLVNYIEP
VKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNKQQLSRIYPKGTRVDSSNY
MPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRRPDKSFDPFTEVI
VDGIVANALRVKVISGQFLSDRKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEE
PFDFPKVVLPTLASLRIAAFEEGGKFVGHRILPVSAIRSGYHYVCLRNEANQPLCLPALL
IYTEASDYIPDDHQDYAEALINPIKHVSLMDQRARQLAALIGESEAQAGQETCQDTQSQQ
LGSQPSSNPTPSPLDASPRRPPGPTTSPASTSLSSPGQRDDLIASILSEVAPTPLDELRG
HKALVKLRSRQERDLRELRKKHQRKAVTLTRRLLDGLAQAQAEGRCRLRPGALGGAADVE
DTKEGEDEAKRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVVLDANTTQ
FKRLKEMNEREKKELQKILDRKRHNSISEAKMRDKHKKEAELTEINRRHITESVNSIRRL
EEAQKQRHDRLVAGQQQVLQQLAEEEPKLLAQLAQECQEQRARLPQEIRRSLLGEMPEGL
GDGPLVACASNGHAPGSSGHLSGADSESQEENTQL

Sequence of entity 3 (E), FASTA

>4GNK_3 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 (chains E)
SPGQRDDLIASILSEVAPTPLDELRGHKALVKLRSRQERDLRELRKKHQRKAVTLTRRLL
DGLAQAQAEGRCRLRPGALGGAADVEDTKEGEDEAKRYQEFQNRQVQSLLELREAQVDAE
AQRRLEHLRQALQRLREVVLDANTTQFKRLKEMNEREKKELQKILDRKRHNSISEAKMRD
KHKKEAELTEINRRHITESVNSIRRLEEAQKQRHDRLVAGQQQVLQQLAEEEPKLLAQLA
QECQEQRARLPQEIRRSLL

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	2
MG	Magnesium ion	Mg	2
ALF	Tetrafluoroaluminate ion	Al F4	2
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	2

Primary citation

Full-length G alpha (q)-phospholipase C-beta 3 structure reveals interfaces of the C-terminal coiled-coil domain. Lyon, A.M., Dutta, S., Boguth, C.A. et al. Nat Struct Mol Biol (2013) 20:355-362. DOI 10.1038/nsmb.2497 · 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…
4QJ3 3.0 Å, Structure of a fragment of human phospholipase C-beta3 delta472-559, in complex with…
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
4EKC 7.4 Å, Structure of human regulator of G protein signaling 2 (RGS2) in complex with murine…

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