9YAP: Gbg crosslinked to PLCb3 - second conformation

Gbg crosslinked to PLCb3 - second conformation. Determined by electron microscopy at 4.5 Å resolution. Released 18 Feb 2026.

Method: Electron microscopy
Resolution: 4.5 Å
Organisms: Homo sapiens, Bos taurus
Chains: 3
Atoms: 8,967
Mol. weight: 144.8 kDa
Released: 18 Feb 2026

Explore 9YAP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9YAP contains 44 α-helices and 65 β-strands across 3 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: 39 helices, 35 β-strands

Element	Residues	Length	Sheet
α-helix	20-24	5
β-strand	26-29	4	1
β-strand	41-43	3	1
β-strand	44-45	2	2
β-strand	51-55	5	2
β-strand	61-65	5	2
β-strand	69-74	6	3
α-helix	84-89	6
α-helix	100-102	3
β-strand	104-108	5	3
β-strand	116-119	4	3
β-strand	121-122	2	1
α-helix	128-139	12
α-helix	142-145	4
α-helix	149-162	14
α-helix	172-178	7
α-helix	184-192	9
α-helix	210-219	10
α-helix	224-233	10
β-strand	241	1	4
α-helix	243-253	11
α-helix	269-278	10
β-strand	291	1	4
α-helix	293-301	9
α-helix	310-313	4
α-helix	323-325	3
β-strand	326	1	5
β-strand	343-344	2	6
α-helix	348-354	7
β-strand	365-366	2	7
α-helix	367-369	3
β-strand	376-377	2	7
β-strand	384-385	2	6
β-strand	387-388	2	7
α-helix	389-398	10
α-helix	419-433	15
α-helix	434-436	3
β-strand	437	1	8
α-helix	441-442	2
α-helix	452-455	4
α-helix	456-459	4
β-strand	463	1	8
α-helix	578-581	4
α-helix	584-587	4
α-helix	588-592	5
β-strand	599	1	9
α-helix	605-611	7
β-strand	617	1	9
α-helix	622-631	10
α-helix	633-640	8
β-strand	644	1	9
α-helix	662-667	6
α-helix	681-689	9
β-strand	700	1	5
α-helix	701-702	2
α-helix	703-706	4
β-strand	727-733	7	10
β-strand	734	1	11
β-strand	735-736	2	10
β-strand	745-752	8	12
α-helix	755-757	3
β-strand	759	1	12
α-helix	765-767	3
β-strand	775	1	11
α-helix	779-781	3
β-strand	783	1	10
β-strand	793-800	8	12
β-strand	804-812	9	12
α-helix	813-815	3
β-strand	821-823	3	10
β-strand	826	1	12
β-strand	837-845	9	10
α-helix	869-877	9
α-helix	878-880	3

Chain B: 3 helices, 30 β-strands

Element	Residues	Length	Sheet
α-helix	3-25	23
α-helix	30-34	5
α-helix	38-39	2
β-strand	47-51	5	13
β-strand	60-62	3	14
β-strand	71-73	3	14
β-strand	78	1	15
β-strand	94	1	15
β-strand	105	1	16
β-strand	111-112	2	16
β-strand	116	1	17
β-strand	121-125	5	16
β-strand	134-139	6	16
β-strand	146-153	8	17
β-strand	156-161	6	17
β-strand	165-170	6	17
β-strand	175-181	7	17
β-strand	187-192	6	18
β-strand	199-203	5	18
β-strand	207-209	3	19
β-strand	221-223	3	19
β-strand	229-234	6	20
β-strand	240-245	6	20
β-strand	250-254	5	20
β-strand	260	1	20
β-strand	264	1	20
β-strand	273-278	6	21
β-strand	284-289	6	21
β-strand	293-298	6	21
β-strand	306-308	3	21
β-strand	317	1	13
β-strand	327-330	4	13
β-strand	336-339	4	13

Chain G: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	9-23	15
α-helix	30-44	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3	A	protein	883	Homo sapiens	Q01970 (AlphaFold model)
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1	B	protein	339	Bos taurus	P62871 (AlphaFold model)
Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2	G	protein	71	Bos taurus	P63212 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9YAP_1 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 (chains A)
MAHHHHHHGTALQLEPPTVVETLRRGSKFIKWDEETSSRNLVTLRVDPNGFFLYWTGPNM
CVDTLDISSIRDTRTGRYARLPKDPKIREVLGFGGPDARLEEKLMTVVSGPDPVNTVFLN
FMAVQDDTAKVWSEELFKLAMNILAQNASRNTFLRKAYTKLKLQVNQDGRIPVKNILKMF
SADKKRVETALESSGLKFNRSESIRPDEFSLEIFERFLNKLSLRPDIDKILLEIGAKGKP
YLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRY
LGGEENGILPLEALDLSTDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGSR
CVELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEAIAETAFKTSPYPVILSFENHVDSA
KQQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKRHRPSAGGPD
SAGRKRPLEQSNSALSESSAATEPSSPQLGSPSSDSCPGLSNGEEVGLEKPSLEPQKSLG
DEGLNRGPYVLGPADREDEEEDEEEEEQTDPKKPTTDEGTASSEVNATEEMSTLVNYIEP
VKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNKQQLSRIYPKGTRVDSSNY
MPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRRPDKSFDPFTEVI
VDGIVANALRVKVISGQFLSDRKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEE
PFDFPKVVLPTLASLRIAAFEEGGKFVGHRILPVSAIRSGYHYVSLRNEANQPLSLPALL
IYTEASDYIPDDHQDYAEALINPIKHVSLMDQRARQLAALIGE

Sequence of entity 2 (B), FASTA

>9YAP_2 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (chains B)
SELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRRTLRGHLAKIYAM
HWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNYVACGGLDNIC
SIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALWDIETGQQTTTFT
GHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDINAICFFPNGNAF
ATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGYDDFNCNVWDALK
ADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN

Sequence of entity 3 (G), FASTA

>9YAP_3 Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (chains G)
MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENP
FREKKFFCAIL

Primary citation

G beta gamma engages PLC beta 3 at multiple sites to reorient and facilitate its activation. Fisher, I.J., Senarath, K., Outlaw, K. et al. bioRxiv (2026). DOI 10.64898/2026.01.14.699417 · PubMed

Other PDB entries of the same protein (UniProt Q01970 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7SQ2 2.6 Å, Reprocessed and refined structure of Phospholipase C-beta and Gq signaling complex
4QJ3 3.0 Å, Structure of a fragment of human phospholipase C-beta3 delta472-559, in complex with…
4QJ4 3.3 Å, Structure of a fragment of human phospholipase C-beta3 delta472-569, bound to IP3 and in…
8EMX 3.3 Å, Phospholipase C beta 3 (PLCb3) in complex with Gbg on lipid nanodiscs
8UQO 3.37 Å, PLCb3-Gbg-Gaq complex on membranes
8UQN 3.4 Å, PLCb3-Gaq complex on membranes
4QJ5 3.41 Å, Structure of a fragment of human phospholipase C-beta3 delta472-581, bound to IP3 and in…
8EMW 3.5 Å, Phospholipase C beta 3 (PLCb3) in complex with Gbg on liposomes
8EMV 3.6 Å, Phospholipase C beta 3 (PLCb3) in solution
4GNK 4.0 Å, Crystal structure of Galphaq in complex with full-length human PLCbeta3
9Y7H 4.4 Å, Gb1g2 crosslinked to PLCb3
9YAO 7.0 Å, Gbg crosslinked to PLCb3 - second conformation

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