4CG5: Cryo-EM of the Sec61-complex

Cryo-EM of the Sec61-complex bound to the 80S ribosome translating a secretory substrate. Determined by electron microscopy at 7.4 Å resolution. Released 5 Feb 2014.

Method: Electron microscopy
Resolution: 7.4 Å
Organism: CANIS LUPUS FAMILIARIS
Chains: 3
Atoms: 4,252
Mol. weight: 64.02 kDa
Released: 5 Feb 2014

Explore 4CG5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4CG5 contains 24 α-helices and 2 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: 17 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	28-51	24
α-helix	62-69	8
β-strand	79	1	1
β-strand	81	1	1
α-helix	83-97	15
α-helix	115-133	19
α-helix	147-169	23
α-helix	178-195	18
α-helix	216-225	10
α-helix	242-259	18
α-helix	284-300	17
α-helix	302-310	9
α-helix	319-322	4
α-helix	341-345	5
α-helix	358-382	25
α-helix	387-397	11
α-helix	406-408	3
α-helix	412-435	24
α-helix	445-465	21

Chain B: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	8-24	17
α-helix	31-51	21
α-helix	52-56	5
α-helix	59-61	3

Chain C: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	75-83	9
α-helix	84-86	3
α-helix	93-95	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein transport protein SEC61 subunit alpha isoform 1	A	protein	476	CANIS LUPUS FAMILIARIS	P38377 (AlphaFold model)
Protein transport protein SEC61 subunit gamma	B	protein	68	CANIS LUPUS FAMILIARIS	P60058 (AlphaFold model)
Protein transport protein SEC61 subunit beta	C	protein	36	CANIS LUPUS FAMILIARIS	P60467 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4CG5_1 PROTEIN TRANSPORT PROTEIN SEC61 SUBUNIT ALPHA ISOFORM 1 (chains A)
MAIKFLEVIKPFCVILPEIQKPERKIQFKEKVLWTAITLFIFLVCCQIPLFGIMSSDSAD
PFYWMRVILASNRGTLMELGISPIVTSGLIMQLLAGAKIIEVGDTPKDRALFNGAQKLFG
MIITIGQSIVYVMTGMYGDPSEMGAGICLLITIQLFVAGLIVLLLDELLQKGYGLGSGIS
LFIATNICETIVWKAFSPTTVNTGRGMEFEGAIIALFHLLATRTDKVRALREAFYRQNLP
NLMNLIATIFVFAVVIYFQGFRVDLPIKSARYRGQYNTYPIKLFYTSNIPIILQSALVSN
LYVISQMLSARFSGNLLVSLLGTWSDTSSGGPARAYPVGGLCHYLSPPESFGSVLEDPVH
AVVYIVFMLGSCAFFSKTWIEVSGSSAKDVAKQLKEQQMVMRGHRETSMVHELNRYIPTA
AAFGGLCIGALSVLADFLGAIGSGTGILLAVTIIYQYFEIFVKEQSEVGSMGALLF

Sequence of entity 2 (B), FASTA

>4CG5_2 PROTEIN TRANSPORT PROTEIN SEC61 SUBUNIT GAMMA (chains B)
MDQVMQFVEPSRQFVKDSIRLVKRCTKPDRKEFQKIAMATAIGFAIMGFIGFFVKLIHIP
INNIIVGG

Sequence of entity 3 (C), FASTA

>4CG5_3 PROTEIN TRANSPORT PROTEIN SEC61 SUBUNIT BETA (chains C)
EDSPGLKVGPVPVLVMSLLFIASVFMLHIWGKYTRS

Primary citation

Structures of the Sec61 Complex Engaged in Nascent Peptide Translocation or Membrane Insertion. Gogala, M., Becker, T., Beatrix, B. et al. Nature (2014) 506:107. DOI 10.1038/NATURE12950 · PubMed

Other PDB entries of the same protein (UniProt P38377 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6Z3T 2.69 Å, Structure of canine Sec61 inhibited by mycolactone
8RJB 2.69 Å, Structure of the rabbit 80S ribosome stalled on a 2-TMD rhodopsin intermediate in…
8RJD 2.79 Å, Structure of the rabbit 80S ribosome stalled on a 2-TMD rhodopsin intermediate in…
8RJC 2.9 Å, Structure of the rabbit 80S ribosome stalled on a 2-TMD rhodopsin intermediate in…
7TM3 3.25 Å, Structure of the rabbit 80S ribosome stalled on a 2-TMD Rhodopsin intermediate in…
8OJ8 3.3 Å, 60S ribosomal subunit bound to the E3-UFM1 complex - state 1 (native)
8BTK 3.5 Å, Structure of the TRAP complex with the Sec translocon and a translating ribosome
3JC2 3.6 Å, The structure of the mammalian Sec61 channel opened by a signal sequence
7TUT 3.88 Å, Structure of the rabbit 80S ribosome stalled on a 4-TMD Rhodopsin intermediate in…
6R7Q 3.9 Å, Structure of XBP1u-paused ribosome nascent chain complex with Sec61.
6FTI 4.2 Å, Cryo-EM Structure of the Mammalian Oligosaccharyltransferase Bound to Sec61 and the…
6FTJ 4.7 Å, Cryo-EM Structure of the Mammalian Oligosaccharyltransferase Bound to Sec61 and the…

Browse structure collections

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