1B9Y: Protein

Structural analysis of phosducin and its phosphorylation-regulated interaction with transducin beta-gamma. Determined by X-ray diffraction at 3.0 Å resolution. Released 23 Feb 1999.

Method
X-ray diffraction
Resolution
3.0 Å
Organisms
Bos taurus, Rattus norvegicus
Chains
3
Atoms
4,526
Mol. weight
74.58 kDa
Ligands
GD
Released
23 Feb 1999

Explore 1B9Y in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1B9Y contains 16 α-helices and 34 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: 4 helices, 29 β-strands

ElementResiduesLengthSheet
α-helix7-2317
α-helix30-334
α-helix38-425
β-strand4311
β-strand47-5152
β-strand58-6363
β-strand69-7463
β-strand78-8363
β-strand88-9473
β-strand100-10564
β-strand111-11664
β-strand121-12554
β-strand137-13934
β-strand146-15385
β-strand156-16165
β-strand166-17055
β-strand175-18065
β-strand187-19266
β-strand198-20366
β-strand207-21266
β-strand218-22366
β-strand229-23467
β-strand240-24567
β-strand250-25457
β-strand259-26467
α-helix2721
β-strand273-27861
β-strand284-28961
β-strand294-29851
β-strand304-30851
β-strand317-32042
β-strand327-33042
β-strand336-33942
Chain B: 4 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix511-52616
α-helix533-54816
α-helix552-5554
α-helix559-5613
Chain C: 8 helices, 5 β-strands
ElementResiduesLengthSheet
α-helix21-3616
α-helix89-10517
β-strand114-11638
α-helix1171
α-helix120-1289
β-strand135-14178
α-helix148-16114
β-strand166-17168
α-helix172-1754
β-strand188-19368
β-strand196-20168
α-helix204-2074
α-helix214-2229

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein (transducin)Aprotein340Bos taurusP62871 (AlphaFold model)
Protein (transducin)Bprotein68Bos taurusP02698 (AlphaFold model)
Protein (phosducin)Cprotein246Rattus norvegicusP20942 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1B9Y_1 PROTEIN (TRANSDUCIN) (chains A)
MSELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRRTLRGHLAKIYA
MHWGTDSRLLLSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNYVACGGLDNI
CSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALWDIETGQQTTTF
TGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDINAICFFPNGNA
FATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGYDDFNCNVWDAL
KADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN
Sequence of entity 2 (B), FASTA
>1B9Y_2 PROTEIN (TRANSDUCIN) (chains B)
MPVINIEDLTEKDKLKMEVDQLKKEVTLERMLVSKCCEEFRDYVEERSGEDPLVKGIPED
KNPFKELK
Sequence of entity 3 (C), FASTA
>1B9Y_3 PROTEIN (PHOSDUCIN) (chains C)
MEEAASQSLEEDFEGQATHTGPKGVINDWRKFKLESEDGDSIPPSKKEILRQMSSPQSRD
DKDSKERMSRKMSIQEYELIHQDKEDEGCLRKYRRQCMQDMHQKLSFGPRYGFVYELETG
EQFLETIEKEQKVTTIVVNIYEDGVRGCDALNSSLECLAAEYPMVKFCKIRASNTGAGDR
FSSDVLPTLLVYKGGELISNFISVAEQFAEDFFAADVESFLNEYGLLPEREIHDLGQTNT
EDEDIE

Ligands and cofactors

IDNameFormulaCopies
GDGadolinium atomGd6

Primary citation

A molecular mechanism for the phosphorylation-dependent regulation of heterotrimeric G proteins by phosducin. Gaudet, R., Savage, J.R., McLaughlin, J.N. et al. Mol Cell (1999) 3:649-660. DOI 10.1016/S1097-2765(00)80358-5 · PubMed

Other PDB entries of the same protein (UniProt P62871 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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