1G4R: Bovine beta-arrestin 1

Crystal structure of bovine beta-arrestin 1. Determined by X-ray diffraction at 2.2 Å resolution. Released 3 Oct 2001.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Bos taurus
Chains: 1
Atoms: 2,900
Mol. weight: 44.31 kDa
Released: 3 Oct 2001

Explore 1G4R in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1G4R contains 8 α-helices and 26 β-strands across 1 chain. 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: 8 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	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	99-108	10
β-strand	112-117	6	1
α-helix	124-126	3
β-strand	127-130	4	3
β-strand	140-151	12	3
α-helix	160-162	3
β-strand	164-168	5	3
β-strand	169-172	4	2
α-helix	180-182	3
β-strand	183-189	7	4
β-strand	196-203	8	4
β-strand	207-209	3	5
β-strand	214-222	9	4
β-strand	228-241	14	6
β-strand	247-258	12	6
β-strand	262	1	6
β-strand	266-274	9	4
β-strand	286-289	4	3
β-strand	300	1	3
α-helix	301-305	5
α-helix	313-315	3
β-strand	317-329	13	6
β-strand	342-349	8	6
β-strand	350-352	3	5
α-helix	353-355	3
β-strand	388-390	3	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Beta-arrestin 1	A	protein	393	Bos taurus	P17870 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1G4R_1 BETA-ARRESTIN 1 (chains A)
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:

1G4M 1.9 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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