1M74: Mg-ADP-bound SecA from Bacillus subtilis

Crystal structure of Mg-ADP-bound SecA from Bacillus subtilis. Determined by X-ray diffraction at 3.0 Å resolution. Released 20 Sept 2002.

Method
X-ray diffraction
Resolution
3.0 Å
Organism
Bacillus subtilis
Chains
1
Atoms
6,501
Mol. weight
92.33 kDa
Ligands
ADP, MG
Released
20 Sept 2002

Explore 1M74 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1M74 contains 40 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: 40 helices, 25 β-strands

ElementResiduesLengthSheet
α-helix4-74
α-helix10-2819
α-helix30-345
α-helix38-5417
α-helix58-7720
α-helix83-9311
β-strand97-9931
α-helix106-11813
β-strand124-12851
α-helix131-14717
β-strand152-15541
α-helix161-1699
β-strand172-17651
α-helix177-18610
α-helix193-1953
β-strand203-20751
α-helix2091
α-helix210-2145
α-helix215-2173
β-strand221-22552
α-helix232-24110
β-strand250-25123
β-strand258-25923
α-helix263-2708
α-helix279-2835
α-helix284-29714
β-strand306-30944
β-strand312-31544
β-strand316-31725
β-strand322-32325
α-helix330-3323
α-helix333-3408
α-helix343-3464
β-strand350-35562
α-helix357-3615
β-strand366-37161
α-helix375-3773
α-helix378-3847
β-strand389-39131
α-helix392-3943
β-strand401-40226
α-helix403-4053
β-strand406-40837
α-helix411-42616
β-strand432-43656
α-helix439-45113
β-strand457-45936
α-helix464-4729
β-strand480-48456
α-helix492-4943
α-helix499-5024
β-strand507-50936
α-helix516-5249
β-strand534-53746
β-strand538-54037
α-helix546-5483
α-helix552-5609
β-strand56917
α-helix572-61847
α-helix624-64219
α-helix657-6648
α-helix681-70323
α-helix707-73529
α-helix748-77730
β-strand794-79742

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Preprotein translocase secAAprotein802Bacillus subtilisP28366 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1M74_1 Preprotein translocase secA (chains A)
MLGILNKMFDPTKRTLNRYEKIANDIDAIRGDYENLSDDALKHKTIEFKERLEKGATTDD
LLVEAFAVVREASRRVTGMFPFKVQLMGGVALHDGNIAEMKTGEGKTLTSTLPVYLNALT
GKGVHVVTVNEYLASRDAEQMGKIFEFLGLTVGLNLNSMSKDEKREAYAADITYSTNNEL
GFDYLRDNMVLYKEQMVQRPLHFAVIDEVDSILIDEARTPLIISGQAAKSTKLYVQANAF
VRTLKAEKDYTYDIKTKAVQLTEEGMTKAEKAFGIDNLFDVKHVALNHHINQALKAHVAM
QKDVDYVVEDGQVVIVDSFTGRLMKGRRYSEGLHQAIEAKEGLEIQNESMTLATITFQNY
FRMYEKLAGMTGTAKTEEEEFRNIYNMQVVTIPTNRPVVRDDRPDLIYRTMEGKFKAVAE
DVAQRYMTGQPVLVGTVAVETSELISKLLKNKGIPHQVLNAKNHEREAQIIEEAGQKGAV
TIATNMAGRGTDIKLGEGVKELGGLAVVGTERHESRRIDNQLRGRSGRQGDPGITQFYLS
MEDELMRRFGAERTMAMLDRFGMDDSTPIQSKMVSRAVESSQKRVEGNNFDSRKQLLQYD
DVLRQQREVIYKQRFEVIDSENLREIVENMIKSSLERAIAAYTPREELPEEWKLDGLVDL
INTTYLDEGALEKSDIFGKEPDEMLELIMDRIITKYNEKEEQFGKEQMREFEKVIVLRAV
DSKWMDHIDAMDQLRQGIHLRAYAQTNPLREYQMEGFAMFEHMIESIEDEVAKFVMKAEI
ENNLEREEVVQGQTTAHQPQEG

Ligands and cofactors

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

Water and common crystallization additives (SO4) are not listed.

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:

Browse structure collections

About this viewer

MolViewer shows 1M74 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.