2WW9: Active yeast Ssh1 complex

Cryo-EM structure of the active yeast Ssh1 complex bound to the yeast 80S ribosome. Determined by electron microscopy at 8.6 Å resolution. Released 8 Dec 2009.

Method
Electron microscopy
Resolution
8.6 Å
Organism
SACCHAROMYCES CEREVISIAE
Chains
15
Atoms
14,301
Mol. weight
261.78 kDa
Released
8 Dec 2009

Explore 2WW9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2WW9 contains 52 α-helices and 36 β-strands across 11 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, 6 β-strands

ElementResiduesLengthSheet
α-helix14-163
α-helix30-4213
α-helix49-502
α-helix53-564
α-helix69-724
α-helix85-10016
α-helix111-13828
α-helix149-17224
α-helix180-19718
α-helix216-22510
α-helix247-26317
β-strand268-26921
β-strand27312
β-strand28012
β-strand285-28621
α-helix288-2914
α-helix293-30513
α-helix315-3195
β-strand33113
β-strand34613
α-helix365-38723
α-helix393-40513
α-helix418-44427
α-helix450-46920
α-helix470-4745
Chain B: 3 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix23-3715
α-helix39-413
α-helix44-7835
Chain C: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix61-7717
Chain H: 9 helices, 4 β-strands
ElementResiduesLengthSheet
α-helix32-4615
α-helix115-12612
α-helix134-1385
β-strand150-15234
α-helix154-1563
α-helix163-17210
α-helix176-1816
α-helix191-1933
β-strand206-20944
β-strand226-22944
α-helix235-2384
β-strand248-25144
α-helix254-2596
Chain I: 4 helices, 5 β-strands
ElementResiduesLengthSheet
α-helix11-133
β-strand14-2295
α-helix26-349
α-helix41-5313
α-helix86-10116
β-strand114-12075
β-strand125-13286
β-strand135-14176
β-strand144-15185
Chain J: 3 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix5-1410
β-strand22-2437
α-helix29-335
α-helix40-478
β-strand50-5237
Chain K: 2 helices, 4 β-strands
ElementResiduesLengthSheet
β-strand63-6648
α-helix70-7910
β-strand81-8668
α-helix92-10312
β-strand107-11378
β-strand120-12678
Chain L: 5 helices, 10 β-strands
ElementResiduesLengthSheet
α-helix2-43
α-helix12-209
β-strand32-3439
α-helix38-436
β-strand47-4939
β-strand55-58410
β-strand67-69310
β-strand70-74511
β-strand79-82411
β-strand89112
β-strand93112
β-strand99111
α-helix101-1033
β-strand104-108510
α-helix115-1195

3 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Sec sixty-one protein homologAprotein490SACCHAROMYCES CEREVISIAEP38353 (AlphaFold model)
Protein transport protein SSS1Bprotein80SACCHAROMYCES CEREVISIAEP35179 (AlphaFold model)
Protein transport protein SEB2Cprotein87SACCHAROMYCES CEREVISIAEP52871 (AlphaFold model)
25S rRNADRNA63SACCHAROMYCES CEREVISIAE
25S rRNAERNA34SACCHAROMYCES CEREVISIAE
25S rRNAFRNA25SACCHAROMYCES CEREVISIAE
25S rRNAGRNA18SACCHAROMYCES CEREVISIAE
60S ribosomal protein L4-BHprotein362SACCHAROMYCES CEREVISIAEP49626 (AlphaFold model)
60S ribosomal protein L17-aIprotein184SACCHAROMYCES CEREVISIAEP05740
60S ribosomal protein L19Jprotein189SACCHAROMYCES CEREVISIAEP0CX82
60S ribosomal protein L25Kprotein142SACCHAROMYCES CEREVISIAEP04456
60S ribosomal protein L26-aLprotein127SACCHAROMYCES CEREVISIAEP05743

3 more molecules are not listed.

Sequence of entity 1 (A), FASTA
>2WW9_1 SEC SIXTY-ONE PROTEIN HOMOLOG (chains A)
MSGFRLIDIVKPILPILPEVELPFEKLPFDDKIVYTIFAGLIYLFAQFPLVGLPKATTPN
VNDPIYFLRGVFGCEPRTLLEFGLFPNISSGLILQLLAGLKVIKVNFKIQSDRELFQSLT
KVFAIVQYVILTNIFIFAGYFGDDLSVVQIGLINFQLVGAGIFTTLLAEVIDKGFGFSSG
AMIINTVVIATNLVADTFGVSQIKVGEDDQTEAQGALINLIQGLRSKHKTFIGGIISAFN
RDYLPNLTTTIIVLAIAIIVCYLQSVRVELPIRSTRARGTNNVYPIKLLYTGCLSVLFSY
TILFYIHIFAFVLIQLVAKNEPTHIICKIMGHYENANNLLAVPTFPLSLLAPPTSFFKGV
TQQPLTFITYSAFILVTGIWFADKWQAISGSSARDVALEFKDQGITLMGRREQNVAKELN
KVIPIAAVTGASVLSLITVIGESLGLKGKAAGIVVGIAGGFSLLEVITIEYQQSGGQSAL
NQVLGVPGAM
Sequence of entity 2 (B), FASTA
>2WW9_2 PROTEIN TRANSPORT PROTEIN SSS1 (chains B)
MARASEKGEEKKQSNNQVEKLVEAPVEFVREGTQFLAKCKKPDLKEYTKIVKAVGIGFIA
VGIIGYAIKLIHIPIRYVIV
Sequence of entity 3 (C), FASTA
>2WW9_3 PROTEIN TRANSPORT PROTEIN SEB2 (chains C)
MAASVPPGGQRILQKRRQAQSIKEKQAKQTPTSTRQAGYGGSSSSILKLYTDEANGFRVD
SLVVLFLSVGFIFSVIALHLLTKFTHI
Sequence of entity 4 (D), FASTA
>2WW9_4 25S RRNA (chains D)
AGAACGCAGCGAAAUGCGAUACGUAAUGUGAAUUGCAGAAUUCCGUGAAUCAUCGAAUCU
UUG
Sequence of entity 5 (E), FASTA
>2WW9_5 25S RRNA (chains E)
UGAAAAGAACUUUGAAAAGAGAGUGAAAAAGUAC
Sequence of entity 6 (F), FASTA
>2WW9_6 25S RRNA (chains F)
CCACGUCAACAGCAGUUGGACGUGG
Sequence of entity 7 (G), FASTA
>2WW9_7 25S RRNA (chains G)
GCCAGCACCUUUGCUGGC
Sequence of entity 8 (H), FASTA
>2WW9_8 60S RIBOSOMAL PROTEIN L4-B (chains H)
MSRPQVTVHSLTGEATANALPLPAVFSAPIRPDIVHTVFTSVNKNKRQAYAVSEKAGHQT
SAESWGTGRAVARIPRVGGGGTGRSGQGAFGNMCRGGRMFAPTKTWRKWNVKVNHNEKRY
ATASAIAATAVASLVLARGHRVEKIPEIPLVVSTDLESIQKTKEAVAALKAVGAHSDLLK
VLKSKKLRAGKGKYRNRRWTQRRGPLVVYAEDNGIVKALRNVPGVETANVASLNLLQLAP
GAHLGRFVIWTEAAFTKLDQVWGSETVASSKVGYTLPSHIISTSDVTRIINSSEIQSAIR
PAGQATQKRTHVLKKNPLKNKQVLLRLNPYAKVFAAEKLGSKKAEKTGTKPAAVFAETLK
HD
Sequence of entity 9 (I), FASTA
>2WW9_9 60S RIBOSOMAL PROTEIN L17-A (chains I)
MARYGATSTNPAKSASARGSYLRVSFKNTRETAQAINGWELTKAQKYLEQVLDHQRAIPF
RRFNSSIGRTAQGKEFGVTKARWPAKSVKFVQGLLQNAAANAEAKGLDATKLYVSHIQVN
QAPKQRRRTYRAHGRINKYESSPSHIELVVTEKEEAVAKAAEKKVVRLTSRQRGRIAAQK
RIAA
Sequence of entity 10 (J), FASTA
>2WW9_10 60S RIBOSOMAL PROTEIN L19 (chains J)
MANLRTQKRLAASVVGVGKRKVWLDPNETSEIAQANSRNAIRKLVKNGTIVKKAVTVHSK
SRTRAHAQSKREGRHSGYGKRKGTREARLPSQVVWIRRLRVLRRLLAKYRDAGKIDKHLY
HVLYKESKGNAFKHKRALVEHIIQAKADAQREKALNEEAEARRLKNRAARDRRAQRVAEK
RDALLKEDA
Sequence of entity 11 (K), FASTA
>2WW9_11 60S RIBOSOMAL PROTEIN L25 (chains K)
MAPSAKATAAKKAVVKGTNGKKALKVRTSATFRLPKTLKLARAPKYASKAVPHYNRLDSY
KVIEQPITSETAMKKVEDGNILVFQVSMKANKYQIKKAVKELYEVDVLKVNTLVRPNGTK
KAYVRLTADYDALDIANRIGYI
Sequence of entity 12 (L), FASTA
>2WW9_12 60S RIBOSOMAL PROTEIN L26-A (chains L)
MAKQSLDVSSDRRKARKAYFTAPSSQRRVLLSAPLSKELRAQYGIKALPIRRDDEVLVVR
GSKKGQEGKISSVYRLKFAVQVDKVTKEKVNGASVPINLHPSKLVITKLHLDKDRKALIQ
RKGGKLE

Primary citation

Structure of Monomeric Yeast and Mammalian Sec61 Complexes Interacting with the Translating Ribosome. Becker, T., Bhushan, S., Jarasch, A. et al. Science (2009) 326:1369. DOI 10.1126/SCIENCE.1178535 · PubMed

Other PDB entries of the same protein (UniProt P38353 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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