1M6N: SecA translocation ATPase from Bacillus subtilis

Crystal structure of the SecA translocation ATPase from Bacillus subtilis. Determined by X-ray diffraction at 2.7 Å resolution. Released 20 Sept 2002.

Method
X-ray diffraction
Resolution
2.7 Å
Organism
Bacillus subtilis
Chains
1
Atoms
6,482
Mol. weight
92.07 kDa
Released
20 Sept 2002

Explore 1M6N in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1M6N contains 41 α-helices and 25 β-strands across 1 chain. 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: 41 helices, 25 β-strands

ElementResiduesLengthSheet
α-helix4-96
α-helix10-2819
α-helix31-344
α-helix38-5316
α-helix58-7720
α-helix83-9412
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-helix2091
α-helix210-2145
α-helix215-2173
β-strand221-22662
α-helix231-24111
β-strand25013
β-strand25913
α-helix264-2674
α-helix270-2723
α-helix279-2835
α-helix284-29815
α-helix302-3054
β-strand306-30724
β-strand314-31524
β-strand31615
β-strand32315
α-helix330-3323
α-helix333-3408
β-strand349-35572
α-helix357-3615
β-strand366-37161
α-helix375-3773
α-helix378-3858
β-strand389-39131
α-helix392-3943
β-strand401-40226
α-helix403-4042
β-strand406-40837
α-helix411-42616
β-strand432-43656
α-helix439-45113
β-strand457-45936
α-helix464-4729
α-helix473-4753
β-strand480-48456
α-helix499-5024
β-strand507-50936
α-helix516-5249
β-strand534-53746
β-strand538-54037
α-helix552-5609
β-strand56917
α-helix572-61847
α-helix624-64118
α-helix649-6513
α-helix656-6649
α-helix681-70222
α-helix707-73428
α-helix748-77730
β-strand794-79742

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Preprotein translocase secAAprotein802Bacillus subtilisP28366 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1M6N_1 Preprotein translocase secA (chains A)
MLGILNKMFDPTKRTLNRYEKIANDIDAIRGDYENLSDDALKHKTIEFKERLEKGATTDD
LLVEAFAVVREASRRVTGMFPFKVQLMGGVALHDGNIAEMKTGEGKTLTSTLPVYLNALT
GKGVHVVTVNEYLASRDAEQMGKIFEFLGLTVGLNLNSMSKDEKREAYAADITYSTNNEL
GFDYLRDNMVLYKEQMVQRPLHFAVIDEVDSILIDEARTPLIISGQAAKSTKLYVQANAF
VRTLKAEKDYTYDIKTKAVQLTEEGMTKAEKAFGIDNLFDVKHVALNHHINQALKAHVAM
QKDVDYVVEDGQVVIVDSFTGRLMKGRRYSEGLHQAIEAKEGLEIQNESMTLATITFQNY
FRMYEKLAGMTGTAKTEEEEFRNIYNMQVVTIPTNRPVVRDDRPDLIYRTMEGKFKAVAE
DVAQRYMTGQPVLVGTVAVETSELISKLLKNKGIPHQVLNAKNHEREAQIIEEAGQKGAV
TIATNMAGRGTDIKLGEGVKELGGLAVVGTERHESRRIDNQLRGRSGRQGDPGITQFYLS
MEDELMRRFGAERTMAMLDRFGMDDSTPIQSKMVSRAVESSQKRVEGNNFDSRKQLLQYD
DVLRQQREVIYKQRFEVIDSENLREIVENMIKSSLERAIAAYTPREELPEEWKLDGLVDL
INTTYLDEGALEKSDIFGKEPDEMLELIMDRIITKYNEKEEQFGKEQMREFEKVIVLRAV
DSKWMDHIDAMDQLRQGIHLRAYAQTNPLREYQMEGFAMFEHMIESIEDEVAKFVMKAEI
ENNLEREEVVQGQTTAHQPQEG

Primary citation

Nucleotide Control of Interdomain Interactions in the Conformational Reaction Cycle of SecA. Hunt, J.F., Weinkauf, S., Henry, L. et al. Science (2002) 297:2018-2026. DOI 10.1126/science.1074424 · 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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