1A0R: Transducin

Heterotrimeric complex of phosducin/transducin beta-gamma. Determined by X-ray diffraction at 2.8 Å resolution. Released 30 Dec 1998.

Method
X-ray diffraction
Resolution
2.8 Å
Organism
Bos taurus
Chains
3
Atoms
4,696
Mol. weight
73.47 kDa
Ligands
FAR
Released
30 Dec 1998

Explore 1A0R in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1A0R contains 19 α-helices and 33 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 B: 5 helices, 28 β-strands

ElementResiduesLengthSheet
α-helix4-2522
α-helix30-334
α-helix38-414
β-strand47-5151
β-strand58-6362
β-strand69-7462
β-strand78-8362
β-strand88-9472
β-strand100-10563
β-strand111-11663
β-strand120-12563
β-strand137-14043
β-strand146-15164
β-strand156-16164
β-strand166-17054
β-strand175-18064
β-strand187-19265
β-strand198-20365
β-strand207-21265
β-strand217-22375
β-strand229-23466
β-strand240-24566
β-strand250-25456
β-strand259-26466
α-helix2721
β-strand273-27867
β-strand284-28967
β-strand294-29857
β-strand304-30857
α-helix309-3113
β-strand317-32041
β-strand327-33041
β-strand336-33941
Chain G: 5 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix6-83
α-helix11-2616
α-helix30-323
α-helix33-4816
α-helix52-554
Chain P: 9 helices, 5 β-strands
ElementResiduesLengthSheet
α-helix21-3515
α-helix74-807
α-helix87-10519
β-strand114-11638
α-helix120-1289
β-strand135-14178
α-helix148-16114
β-strand166-17168
α-helix172-1754
α-helix1861
β-strand188-19368
β-strand196-20168
α-helix204-2074
α-helix214-2229

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transducin (beta subunit)Bprotein340Bos taurusP62871 (AlphaFold model)
Transducin (gamma subunit)Gprotein65Bos taurusP02698 (AlphaFold model)
PhosducinPprotein245Bos taurusP19632 (AlphaFold model)
Sequence of entity 1 (B), FASTA
>1A0R_1 TRANSDUCIN (BETA SUBUNIT) (chains B)
XSELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRRTLRGHLAKIYA
MHWGTDSRLLLSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNYVACGGLDNI
CSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALWDIETGQQTTTF
TGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDINAICFFPNGNA
FATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGYDDFNCNVWDAL
KADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN
Sequence of entity 2 (G), FASTA
>1A0R_2 TRANSDUCIN (GAMMA SUBUNIT) (chains G)
PVINIEDLTEKDKLKMEVDQLKKEVTLERMLVSKCCEEFRDYVEERSGEDPLVKGIPEDK
NPFKE
Sequence of entity 3 (P), FASTA
>1A0R_3 PHOSDUCIN (chains P)
MEKAKSQSLEEDFEGQASHTGPKGVINDWRKFKLESEDSDSVAHSKKEILRQMSSPQSRD
DKDSKERFSRKMSVQEYELIHKDKEDENCLRKYRRQCMQDMHQKLSFGPRYGFVYELESG
EQFLETIEKEQKITTIVVHIYEDGIKGCDALNSSLICLAAEYPMVKFCKIKASNTGAGDR
FSSDVLPTLLVYKGGELLSNFISVTEQLAEEFFTGDVESFLNEYGLLPEKEMHVLEQTNM
EEDME

Ligands and cofactors

IDNameFormulaCopies
FARFarnesylC15 H261

Primary citation

Phosducin induces a structural change in transducin beta gamma. Loew, A., Ho, Y.K., Blundell, T. et al. Structure (1998) 6:1007-1019. DOI 10.1016/S0969-2126(98)00102-6 · 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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