9KY2: Beta-arrestin2

Structure of beta-arrestin2 in complex with mouse C5aR1pp. Determined by electron microscopy at 2.78 Å resolution. Released 26 Nov 2025.

Method: Electron microscopy
Resolution: 2.78 Å
Organisms: Bos taurus, Mus musculus
Chains: 8
Atoms: 9,346
Mol. weight: 198.11 kDa
Released: 26 Nov 2025

Explore 9KY2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9KY2 contains 29 α-helices and 109 β-strands across 8 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: 10 helices, 29 β-strands

Element	Residues	Length	Sheet
β-strand	8-13	6	1
β-strand	20-23	4	1
β-strand	27-29	3	2
β-strand	30	1	3
β-strand	35	1	3
β-strand	38-43	6	1
β-strand	53-64	12	4
β-strand	75-88	14	4
α-helix	91	1
α-helix	100-109	10
β-strand	113-118	6	1
α-helix	124-126	3
β-strand	128-130	3	4
α-helix	131-133	3
β-strand	142-152	11	4
α-helix	158-159	2
β-strand	164-169	6	4
β-strand	170-172	3	2
α-helix	181-183	3
β-strand	185-190	6	5
β-strand	197-202	6	5
β-strand	204	1	6
β-strand	208-210	3	7
β-strand	215-219	5	6
β-strand	220-223	4	5
β-strand	229-243	15	8
β-strand	247-259	13	8
β-strand	263	1	8
β-strand	267-268	2	5
β-strand	271-275	5	6
β-strand	289-291	3	4
α-helix	292-293	2
β-strand	301	1	4
α-helix	302-304	3
β-strand	317-330	14	8
β-strand	336-342	7	8
β-strand	343-345	3	7
α-helix	347-349	3
α-helix	394-407	14

Chain B: 1 helix, 13 β-strands

Element	Residues	Length	Sheet
β-strand	6-10	5	9
β-strand	14	1	10
β-strand	19-28	10	9
β-strand	35-42	8	11
β-strand	48-55	8	11
β-strand	60-63	4	11
β-strand	68	1	9
β-strand	71-76	6	9
β-strand	81-89	9	9
α-helix	91-93	3
β-strand	95-103	9	11
β-strand	112-113	2	11
β-strand	117-119	3	11
β-strand	120	1	10

Chains C and E: 3 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	5-8	4	12
β-strand	11-13	3	13
β-strand	20-26	7	12
β-strand	34-39	6	13
β-strand	47-50	4	13
β-strand	54-55	2	13
α-helix	56	1
β-strand	63-68	6	12
β-strand	71-76	6	12
α-helix	81-83	3
β-strand	86-91	6	13
α-helix	97	1
β-strand	98-99	2	13
β-strand	103-106	4	13

Chain D: 1 helix, 13 β-strands

Element	Residues	Length	Sheet
β-strand	6-10	5	14
β-strand	14-15	2	15
β-strand	19-28	10	14
β-strand	35-42	8	16
β-strand	48-55	8	16
β-strand	60-63	4	16
β-strand	68	1	14
β-strand	71-76	6	14
β-strand	81-89	9	14
α-helix	91-93	3
β-strand	95-103	9	16
β-strand	112-113	2	16
β-strand	117-119	3	16
β-strand	120-121	2	15

Chain F: 9 helices, 30 β-strands

Element	Residues	Length	Sheet
β-strand	8-13	6	19
β-strand	19-23	5	19
β-strand	27-29	3	20
β-strand	30	1	21
β-strand	35	1	21
β-strand	38-44	7	19
β-strand	53-64	12	22
β-strand	73-75	3	4
β-strand	76-88	13	22
α-helix	91	1
α-helix	100-109	10
β-strand	113-118	6	19
α-helix	124-126	3
β-strand	128-130	3	22
α-helix	131-133	3
β-strand	141-152	12	22
α-helix	158-159	2
β-strand	165-169	5	22
β-strand	170-172	3	20
α-helix	181-183	3
β-strand	185-190	6	23
β-strand	197-202	6	23
β-strand	204	1	24
β-strand	208-210	3	25
β-strand	215-219	5	24
β-strand	220-223	4	23
β-strand	229-243	15	26
β-strand	247-259	13	26
β-strand	263	1	26
β-strand	267-268	2	23
β-strand	271-275	5	24
β-strand	289-291	3	22
β-strand	301	1	22
α-helix	302-306	5
β-strand	317-330	14	26
β-strand	336-342	7	26
β-strand	343-345	3	25
α-helix	347-349	3
α-helix	394-406	13

Chains U and V: 1 helix, 1 β-strand

Element	Residues	Length	Sheet
α-helix	337-338	2
β-strand	341-344	4	19

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Beta-arrestin-2	A, F	protein	420	Bos taurus	P32120 (AlphaFold model)
Fab30 Heavy Chain	B, D	protein	237	Mus musculus
Fab30 Light Chain	C, E	protein	215	Mus musculus
C5a anaphylatoxin chemotactic receptor 1	U, V	protein	23	Mus musculus	P30993 (AlphaFold model)

Sequence of entity 1 (A, F), FASTA

>9KY2_1 Beta-arrestin-2 (chains A, F)
MGEKPGTRVFKKSSPNGKLTVYLGKRDFVDHLDKVDPVDGVVLVDPDYLKDRKVFVTLTV
AFRYGREDCDVLGLSFRKDLFIANYQAFPPTPNPPRPPTRLQERLLRKLGQHAHPFFFTI
PQNLPSSVTLQPGPEDTGKALGVDFEIRAFVAKSLEEKSHKRNSVRLVIRKVQFAPEKPG
PQPSAETTRHFLMSDRSLHLEASLDKELYYHGEPLNVNVHVTNNSTKTVKKIKVSVRQYA
DIVLFSTAQYKVPVAQVEQDDQVSPSSTFSKVYTITPFLANNREKRGLALDGKLKHEDTN
LASSTIVKEGANKEVLGILVSYRVKVKLVVSRGGDVSVELPFVLMHPKPHDHIALPRPQS
AATHPPTLLPSAVPETDAPVDTNLIEFETNYATDDDIVFEDFARLRLKGLKDEDYDDQFC

Sequence of entity 2 (B, D), FASTA

>9KY2_2 Fab30 Heavy Chain (chains B, D)
EISEVQLVESGGGLVQPGGSLRLSCAASGFNVYSSSIHWVRQAPGKGLEWVASISSYYGY
TYYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARSRQFWYSGLDYWGQGTLVT
VSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL
QSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHHHHHHHH

Sequence of entity 3 (C, E), FASTA

>9KY2_3 Fab30 Light Chain (chains C, E)
SDIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVP
SRFSGSRSGTDFTLTISSLQPEDFATYYCQQYKYVPVTFGQGTKVEIKRTVAAPSVFIFP
PSDSQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL
TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

Sequence of entity 4 (U, V), FASTA

>9KY2_4 C5a anaphylatoxin chemotactic receptor 1 (chains U, V)
GGGDSKTFTPSTTDTSTRKSQAV

Primary citation

Molecular fingerprints of a convergent mechanism orchestrating diverse ligand recognition and species-specific pharmacology at the complement anaphylatoxin receptors. Mishra, S., Yadav, M.K., Dalal, A. et al. bioRxiv (2025). DOI 10.1101/2025.05.26.656101 · PubMed

Other PDB entries of the same protein (UniProt P32120 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5TV1 2.4 Å, active arrestin-3 with inositol hexakisphosphate
8J8R 2.9 Å, Structure of beta-arrestin2 in complex with M2Rpp
3P2D 3.0 Å, Crystal structure of arrestin-3 reveals the basis of the difference in receptor binding…
8J8V 3.22 Å, Structure of beta-arrestin2 in complex with D6Rpp (Local Refine)
8VJ9 3.3 Å, CryoEM structure of human ACKR3 phosphorylated by GRK5 in complex with Arrestin3 variant…
8GO9 3.35 Å, Structure of beta-arrestin2 in complex with a phosphopeptide corresponding to the human…
8TIL 3.8 Å, Human ACKR3 phosphorylated by GRK5 in complex with Arrestin3 reconstructed without…
8I10 3.96 Å, Structure of beta-arrestin2 in complex with a phosphopeptide corresponding to the human…
8TIN 4.0 Å, Human ACKR3 phosphorylated by GRK2 in complex with Arrestin3 reconstructed without…
8GOC 4.18 Å, Structure of beta-arrestin2 in complex with a phosphopeptide corresponding to the human…
8I0Z 4.33 Å, Structure of beta-arrestin2 in complex with a phosphopeptide corresponding to the human…
8GOO 4.4 Å, Structure of beta-arrestin2 in complex with a phosphopeptide corresponding to the human…

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