1TAD: Transducin-alpha

Gtpase mechanism of gproteins from the 1.7-Å crystal structure of transducin alpha-GDP-ALF4-. Determined by X-ray diffraction at 1.7 Å resolution. Released 8 May 1995.

Method
X-ray diffraction
Resolution
1.7 Å
Organism
Bos taurus
Chains
3
Atoms
8,773
Mol. weight
114.01 kDa
Ligands
CAC, ALF, GDP, CA
Released
8 May 1995

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

Secondary structure: helices and β-sheets

1TAD contains 60 α-helices and 25 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: 19 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand28-3581
α-helix42-5312
α-helix59-8628
α-helix96-10914
α-helix1111
α-helix117-12812
α-helix130-1378
α-helix139-1413
α-helix148-1525
α-helix155-1584
α-helix167-1726
β-strand181-18771
β-strand190-19671
α-helix201-2044
α-helix207-2104
β-strand216-22271
α-helix223-2275
β-strand22912
β-strand23712
α-helix238-25013
α-helix253-2553
β-strand259-26571
α-helix267-2737
α-helix279-2813
α-helix292-30413
β-strand316-31941
α-helix325-34117
Chain B: 21 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand29-3683
α-helix42-5312
α-helix59-8628
α-helix89-913
α-helix96-10914
α-helix1111
α-helix117-12812
α-helix130-1367
α-helix139-1413
α-helix148-1525
α-helix155-1584
α-helix167-1726
β-strand181-18773
β-strand190-19673
α-helix201-2044
α-helix207-2104
β-strand216-22273
α-helix223-2275
β-strand22914
β-strand23714
α-helix238-25013
α-helix253-2553
β-strand259-26573
α-helix267-2737
α-helix279-2813
α-helix292-30413
α-helix314-3152
β-strand316-31943
α-helix325-34117
Chain C: 20 helices, 9 β-strands
ElementResiduesLengthSheet
β-strand28-3585
α-helix42-5312
α-helix59-635
α-helix65-8622
α-helix95-10713
α-helix1111
α-helix117-12711
α-helix130-1378
α-helix139-1413
α-helix148-1536
α-helix155-1595
β-strand16311
α-helix167-1726
β-strand181-18775
β-strand190-19675
α-helix201-2044
α-helix205-2106
β-strand216-22275
α-helix223-2275
β-strand22916
β-strand23716
α-helix238-25013
α-helix253-2553
β-strand259-26575
α-helix267-2737
α-helix279-2813
α-helix292-30413
β-strand316-31945
α-helix325-34218

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transducin-alphaA, B, Cprotein324Bos taurusP04695 (AlphaFold model)
Sequence of entity 1 (A, B, C), FASTA
>1TAD_1 TRANSDUCIN-ALPHA (chains A, B, C)
ARTVKLLLLGAGESGKSTIVKQMKIIHQDGYSLEECLEFIAIIYGNTLQSILAIVRAMTT
LNIQYGDSARQDDARKLMHMADTIEEGTMPKEMSDIIQRLWKDSGIQACFDRASEYQLND
SAGYYLSDLERLVTPGYVPTEQDVLRSRVKTTGIIETQFSFKDLNFRMFDVGGQRSERKK
WIHCFEGVTCIIFIAALSAYDMVLVEDDEVNRMHESLHLFNSICNHRYFATTSIVLFLNK
KDVFSEKIKKAHLSICFPDYNGPNTYEDAGNYIKVQFLELNMRRDVKEIYSHMTCATDTQ
NVKFVFDAVTDIIIKENLKDCGLF

Ligands and cofactors

IDNameFormulaCopies
CACCacodylate ionC2 H6 As O26
ALFTetrafluoroaluminate ionAl F43
GDPGuanosine-5'-diphosphateC10 H15 N5 O11 P23
CACalcium ionCa3

Primary citation

GTPase mechanism of Gproteins from the 1.7-A crystal structure of transducin alpha-GDP-AIF-4. Sondek, J., Lambright, D.G., Noel, J.P. et al. Nature (1994) 372:276-279. DOI 10.1038/372276a0 · PubMed

Other PDB entries of the same protein (UniProt P04695 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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