1G4M: Bovine beta-arrestin 1

Crystal structure of bovine beta-arrestin 1. Determined by X-ray diffraction at 1.9 Å resolution. Released 3 Oct 2001.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Bos taurus
Chains: 2
Atoms: 5,926
Mol. weight: 88.62 kDa
Released: 3 Oct 2001

Explore 1G4M in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1G4M contains 20 α-helices and 56 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: 11 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	6-12	7	1
β-strand	19-22	4	1
β-strand	26-29	4	2
β-strand	34	1	2
β-strand	37-42	6	1
α-helix	45-48	4
β-strand	52-63	12	3
β-strand	75-87	13	3
α-helix	99-107	9
β-strand	112-117	6	1
α-helix	124-126	3
β-strand	127-130	4	3
α-helix	133-138	6
β-strand	140-151	12	3
α-helix	157-159	3
α-helix	160-162	3
β-strand	163-168	6	3
β-strand	169-172	4	2
α-helix	181-184	4
β-strand	185-189	5	4
β-strand	191	1	5
β-strand	197-203	7	4
β-strand	207-209	3	6
β-strand	214-222	9	4
β-strand	228-241	14	7
β-strand	245	1	8
β-strand	247-258	12	7
β-strand	262	1	7
β-strand	266-274	9	4
α-helix	278-280	3
β-strand	287-289	3	3
β-strand	300	1	3
α-helix	301-304	4
α-helix	313-315	3
β-strand	317-329	13	7
β-strand	342-349	8	7
β-strand	350-352	3	6
α-helix	353-355	3
β-strand	386-390	5	1

Chain B: 9 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	6-12	7	9
β-strand	18-22	5	9
β-strand	26-29	4	10
β-strand	34	1	10
β-strand	37-43	7	9
α-helix	45-48	4
β-strand	52-63	12	11
β-strand	75-87	13	11
α-helix	99-105	7
β-strand	112-117	6	9
α-helix	124-126	3
β-strand	127-129	3	11
β-strand	140-151	12	11
α-helix	160-162	3
β-strand	163-168	6	11
β-strand	169-172	4	10
α-helix	175-177	3
α-helix	181-184	4
β-strand	185-189	5	12
β-strand	191	1	8
β-strand	197-203	7	12
β-strand	207-209	3	13
β-strand	214-222	9	12
β-strand	228-241	14	14
β-strand	245	1	5
β-strand	247-258	12	14
β-strand	262	1	14
β-strand	266-274	9	12
β-strand	288-289	2	11
β-strand	300	1	11
α-helix	301-305	5
α-helix	313-315	3
β-strand	317-330	14	14
β-strand	340-349	10	14
β-strand	350-352	3	13
α-helix	353-355	3
β-strand	386-390	5	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Beta-ARRESTIN1	A, B	protein	393	Bos taurus	P17870 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1G4M_1 BETA-ARRESTIN1 (chains A, B)
MGDKGTRVFKKASPNGKLTVYLGKRDFVDHIDLVEPVDGVVLVDPEYLKERRVYVTLTCA
FRYGREDLDVLGLTFRKDLFVANVQSFPPAPEDKKPLTRLQERLIKKLGEHAYPFTFEIP
PNLPCSVTLQPGPEDTGKACGVDYEVKAFCAENLEEKIHKRNSVRLVIRKVQYAPERPGP
QPTAETTRQFLMSDKPLHLEASLDKEIYYHGEPISVNVHVTNNTNKTVKKIKISVRQYAD
ICLFNTAQYKCPVAMEEADDTVAPSSTFCKVYTLTPFLANNREKRGLALDGKLKHEDTNL
ASSTLLREGANREILGIIVSYKVKVKLVVSRGGLLGDLASSDVAVELPFTLMHPKPKEEP
PHREVPEHETPVDTNLIELDTNDDDIVFEDFAR

Primary citation

Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation. Han, M., Gurevich, V.V., Vishnivetskiy, S.A. et al. Structure (2001) 9:869-880. DOI 10.1016/S0969-2126(01)00644-X · PubMed

Other PDB entries of the same protein (UniProt P17870 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1G4R 2.2 Å, Crystal structure of bovine beta-arrestin 1
3GC3 2.2 Å, Crystal Structure of Arrestin2S and Clathrin
7DFC 2.49 Å, Crystal of Arrestin2-V2Rpp-3-Fab30 complex
7DFA 2.54 Å, Crystal of Arrestin2-V2Rpp-4-Fab30 complex
22GM 2.7 Å, C5a bound C5aR1 in complex with beta-arrestin1
9WSV 2.8 Å, Cryo-EM structure of DAMGO-muOR-arrestin-1-Fab30 complex
9WSX 2.8 Å, Cryo-EM structure of endomorphin-1-muOR-arrestin2-Fab30 complex
22GK 2.84 Å, C5a bound C5aR2 in complex with beta-arrestin1
1JSY 2.9 Å, Crystal structure of bovine arrestin-2
1ZSH 2.9 Å, Crystal structure of bovine arrestin-2 in complex with inositol hexakisphosphate (IP6)
22CR 2.9 Å, C5a-desArg bound C5aR2 in complex with beta-arrestin1
2WTR 2.9 Å, Full length Arrestin2

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