5EUL: PDB entry 5EUL

Structure of the SecA-SecY complex with a translocating polypeptide substrate. Determined by X-ray diffraction at 3.7 Å resolution. Released 9 Mar 2016.

Method
X-ray diffraction
Resolution
3.7 Å
Organisms
Bacillus subtilis (strain 168), synthetic construct, Bacillus subtilis
Chains
4
Atoms
10,511
Mol. weight
201.17 kDa
Ligands
BEF, TBR, ADP, MG
Released
9 Mar 2016

Explore 5EUL in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5EUL contains 57 α-helices and 45 β-strands across 4 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: 38 helices, 25 β-strands

ElementResiduesLengthSheet
α-helix16-2813
α-helix31-344
α-helix37-5317
α-helix58-7619
α-helix79-824
α-helix83-9311
β-strand97-9931
α-helix106-11813
β-strand124-12851
α-helix131-14717
β-strand152-15431
α-helix161-1699
β-strand172-17651
α-helix177-18711
α-helix193-1953
β-strand203-20751
α-helix209-2102
α-helix211-2155
β-strand220-22672
α-helix234-2407
β-strand25113
β-strand25813
α-helix263-27210
α-helix281-2833
α-helix286-29813
β-strand30314
β-strand306-30944
β-strand312-31654
α-helix3171
β-strand323-32424
α-helix333-3408
α-helix347-3482
β-strand349-35682
α-helix357-3615
β-strand367-37151
α-helix374-3774
α-helix378-3836
β-strand389-39131
β-strand401-40225
α-helix403-4053
β-strand406-40836
α-helix412-42716
β-strand432-43545
α-helix439-45012
β-strand457-45935
α-helix467-4748
β-strand480-48345
α-helix485-4873
α-helix500-5023
β-strand506-50945
α-helix516-5249
β-strand534-53745
β-strand538-54036
α-helix544-5474
α-helix554-5607
β-strand56916
α-helix572-61847
α-helix626-64116
α-helix685-69814
α-helix707-73630
α-helix754-76916
β-strand77017
α-helix797-82327
Chain E: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix3-1715
α-helix24-5431
Chain V: 1 helix, 14 β-strands
ElementResiduesLengthSheet
β-strand5-7311
β-strand11-12212
β-strand18-24711
β-strand33-37513
β-strand47-52613
β-strand57-58213
β-strand67-72611
β-strand76-82711
α-helix87-893
β-strand91-93314
β-strand94-98513
β-strand106113
β-strand109111
β-strand111-113314
β-strand114-115212
Chain Y: 16 helices, 6 β-strands
ElementResiduesLengthSheet
α-helix14-3017
α-helix31-333
α-helix41-444
β-strand5718
β-strand6019
β-strand6319
β-strand6618
α-helix75-8814
α-helix93-997
α-helix104-13532
α-helix148-17023
α-helix178-18811
α-helix192-1965
α-helix217-23519
β-strand238-242510
β-strand261-265510
α-helix276-28813
α-helix290-2923
α-helix309-33022
α-helix335-3428
α-helix354-38532
α-helix400-42021

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein translocase subunit SecA, Insertion Peptide ChimeraAprotein836Bacillus subtilis (strain 168), synthetic construct, Bacillus subtilisP28366 (AlphaFold model)
Protein translocase subunit SecYYprotein424Geobacillus thermodenitrificans (strain NG80-2)A4IJK8 (AlphaFold model)
Preprotein translocase SecE subunitEprotein70Geobacillus thermodenitrificans (strain NG80-2)A4IJH4 (AlphaFold model)
AYC08Vprotein131Vicugna pacos
Sequence of entity 1 (A), FASTA
>5EUL_1 Protein translocase subunit SecA, Insertion Peptide Chimera (chains A)
MLGILNKMFDPTKRTLNRYEKIANDIDAIRGDYENLSDDALKHKTIEFKERLEKGATTDD
LLVEAFAVVREASRRVTGMFPFKVQLMGGVALHDGNIAEMKTGEGKTLTSTLPVYLNALT
GKGVHVVTVNEYLASRDAEQMGKIFEFLGLTVGLNLNSMSKDEKREAYAADITYSTNNEL
GFDYLRDNMVLYKEQMVQRPLHFAVIDEVDSILIDEARTPLIISGQAAKSTKLYVQANAF
VRTLKAEKDYTYDIKTKAVQLTEEGMTKAEKAFGIDNLFDVKHVALNHHINQALKAHVAM
QKDVDYVVEDGQVVIVDSFTGRLMKGRRYSEGLHQAIEAKEGLEIQNESMTLATITFQNY
FRMYEKLAGMTGTAKTEEEEFRNIYNMQVVTIPTNRPVVRDDRPDLIYRTMEGKFKAVAE
DVAQRYMTGQPVLVGTVAVETSELISKLLKNKGIPHQVLNAKNHEREAQIIEEAGQKGAV
TIATNMAGRGTDIKLGEGVKELGGLAVVGTERHESRRIDNQLRGRSGRQGDPGITQFYLS
MEDELMRRFGAERTMAMLDRFGMDDSTPIQSKMVSRAVESSQKRVEGNNFDSRKQLLQYD
DVLRQQREVIYKQRFEVIDSENLREIVENMIKSSLERAIAAYTPREELPEEWKLDGLVDL
INTTYLDEGALEKSDIFGKEPDEMLELIMDRIITKYNEKEEQFGKEQMREFEKVIVLRAV
DSKWMDHIDAMDQLRQGIHLRGSGGSGGKKTAIAIAVALAGFATVASYAQYEDGCSGELE
RQHTFAGGPGAQTNPLREYQMEGFAMFEHMIESIEDEVAKFVMKAEITSLEVLFQG
Sequence of entity 2 (Y), FASTA
>5EUL_2 Protein translocase subunit SecY (chains Y)
MFRTISNFMRVSDIRNKIIFTLLMLIVFRIGTFIPVPSVNTDVLKLQDQLNAFGVLNIFC
GGALQNFSIFAMGVMPYITASIIVQLLQMDVVPKFAEWSKQGEMGRRKLAQFTRYFTIVL
GFIQALGMSYGFNNLAGGMLIQNPGIGTYLLIAVVLTAGTAFLMWLGEQITAKGVGNGIS
IIIFAGIVSGIPTILNQIYAQTFGGLNIVRLLLVALAVVAVIVGVIYIQQAFRKIPIQYA
KRLEGRNPVGGHSTHLPLKVNPAGVIPVIFAVSFLIAPPTIASFFGTNDVTLWIRRTFDY
THPVGMTIYVVLIIAFTYFYAFVQVNPEQMADNLKKQGGYIPGIRPGKNTQEYVTRILYR
LTLVGSLFLAFIAVLPVFFVNFANLPPSAQIGGTSLLIVVGVALETMKQLESQLVKRHYR
GFIK
Sequence of entity 3 (E), FASTA
>5EUL_3 Preprotein translocase SecE subunit (chains E)
MQRVTNFFKEVVRELKKVSWPNRKELVNYTAVVLATVAFFTVFFAVIDLGISQLIRLVFE
GGHHHHHHHH
Sequence of entity 4 (V), FASTA
>5EUL_4 AYC08 (chains V)
QVQLVETGGGLVQPGGSLRLSCGASGSIFNMYAMGWYRQAPGKQREVVARIATDDSTMYP
DSVKGRFTISRDNAKNTVYLQMNSLKPEDTAVYYCYYQRTVMSQPYWGQGTQVTVSSGGL
PETGGHHHHHH

Ligands and cofactors

IDNameFormulaCopies
BEFBeryllium trifluoride ionBe F31
TBRHexatantalum dodecabromideBr12 Ta618
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P21
MGMagnesium ionMg1

Primary citation

Crystal structure of a substrate-engaged SecY protein-translocation channel. Li, L., Park, E., Ling, J. et al. Nature (2016) 531:395-399. DOI 10.1038/nature17163 · PubMed

Other PDB entries of the same protein (UniProt P28366 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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