1TF2: Preprotein translocase secA subunit

Crystal structure of SecA:ADP in an open conformation from Bacillus Subtilis. Determined by X-ray diffraction at 2.9 Å resolution. Released 3 Aug 2004.

Method
X-ray diffraction
Resolution
2.9 Å
Organism
Bacillus subtilis
Chains
1
Atoms
6,217
Mol. weight
96.41 kDa
Ligands
ADP, MG
Released
3 Aug 2004

Explore 1TF2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1TF2 contains 41 α-helices and 27 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, 27 β-strands

ElementResiduesLengthSheet
α-helix1-66
α-helix18-2811
α-helix29-313
α-helix38-5417
α-helix58-7720
α-helix83-9311
β-strand97-9931
α-helix106-11813
β-strand124-12851
α-helix131-14717
β-strand152-15431
α-helix161-1677
β-strand172-17651
α-helix177-18711
α-helix193-1953
β-strand203-20751
α-helix209-2102
α-helix211-2155
α-helix2191
β-strand220-22452
α-helix232-24110
β-strand250-25233
β-strand259-26133
α-helix263-27210
α-helix281-2833
α-helix284-29815
β-strand30214
β-strand306-30944
β-strand312-31544
β-strand31615
β-strand32315
α-helix333-3408
α-helix347-3493
β-strand351-35662
α-helix357-3615
β-strand366-37161
α-helix375-3773
α-helix378-3858
β-strand389-39131
α-helix392-3943
β-strand401-40226
α-helix403-4053
β-strand406-40837
α-helix411-42818
β-strand432-43656
α-helix439-45012
β-strand457-45936
α-helix464-4729
β-strand480-48456
α-helix494-4963
α-helix500-5023
β-strand505-50956
α-helix516-5238
β-strand533-53756
β-strand538-54037
α-helix545-5473
α-helix550-56112
β-strand56418
β-strand56718
β-strand56917
α-helix572-61847
α-helix624-64219
α-helix657-6626
α-helix681-69717
α-helix698-7025
α-helix7031
α-helix705-73632
α-helix748-77629

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Preprotein translocase secA subunitAprotein844Bacillus subtilisP28366 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1TF2_1 Preprotein translocase secA subunit (chains A)
GPHMLGILNKMFDPTKRTLNRYEKIANDIDAIRGDYENLSDDALKHKTIEFKERLEKGAT
TDDLLVEAFAVVREASRRVTGMFPFKVQLMGGVALHDGNIAEMKTGEGKTLTSTLPVYLN
ALTGKGVHVVTVNEYLASRDAEQMGKIFEFLGLTVGLNLNSMSKDEKREAYAADITYSTN
NELGFDYLRDNMVLYKEQMVQRPLHFAVIDEVDSILIDEARTPLIISGQAAKSTKLYVQA
NAFVRTLKAEKDYTYDIKTKAVQLTEEGMTKAEKAFGIDNLFDVKHVALNHHINQALKAH
VAMQKDVDYVVEDGQVVIVDSFTGRLMKGRRYSEGLHQAIEAKEGLEIQNESMTLATITF
QNYFRMYEKLAGMTGTAKTEEEEFRNIYNMQVVTIPTNRPVVRDDRPDLIYRTMEGKFKA
VAEDVAQRYMTGQPVLVGTVAVETSELISKLLKNKGIPHQVLNAKNHEREAQIIEEAGQK
GAVTIATNMAGRGTDIKLGEGVKELGGLAVVGTERHESRRIDNQLRGRSGRQGDPGITQF
YLSMEDELMRRFGAERTMAMLDRFGMDDSTPIQSKMVSRAVESSQKRVEGNNFDSRKQLL
QYDDVLRQQREVIYKQRFEVIDSENLREIVENMIKSSLERAIAAYTPREELPEEWKLDGL
VDLINTTYLDEGALEKSDIFGKEPDEMLELIMDRIITKYNEKEEQFGKEQMREFEKVIVL
RAVDSKWMDHIDAMDQLRQGIHLRAYAQTNPLREYQMEGFAMFEHMIESIEDEVAKFVMK
AEIENNLEREEVVQGQTTAHQPQEGDDNKKAKKAPVRKVVDIGRNAPCHCGSGKKYKNCC
GRTE

Ligands and cofactors

IDNameFormulaCopies
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P21
MGMagnesium ionMg1

Primary citation

A large conformational change of the translocation ATPase SecA. Osborne, A.R., Clemons Jr., W.M., Rapoport, T.A. Proc Natl Acad Sci U S A (2004) 101:10937-10942. DOI 10.1073/pnas.0401742101 · PubMed

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

Browse structure collections

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