13JG: E. coli DnaK

E. coli DnaK bound to peptide PA1, structure B. Determined by X-ray diffraction at 1.52 Å resolution. Released 27 May 2026.

Method
X-ray diffraction
Resolution
1.52 Å
Organism
Escherichia coli
Chains
1
Atoms
1,978
Mol. weight
24.85 kDa
Ligands
A1DFX
Released
27 May 2026

Explore 13JG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

13JG contains 9 α-helices and 11 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: 9 helices, 11 β-strands

ElementResiduesLengthSheet
β-strand39411
β-strand399-40352
β-strand407-41262
α-helix4161
β-strand41711
β-strand420-42673
β-strand436-44272
β-strand44712
α-helix448-4503
β-strand452-45982
α-helix462-4632
β-strand472-47873
β-strand484-49073
β-strand496-50163
α-helix509-52113
α-helix523-55331
α-helix554-5563
α-helix559-57618
α-helix581-59414
α-helix596-6049

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Chaperone protein DnaKAprotein219Escherichia coliP0A6Y8 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>13JG_1 Chaperone protein DnaK (chains A)
VLLLDVTPLSLGIETMGGVMTTLIAKNTTIPTKHSQVFSTAEDNQSAVTIHVLQGERKRA
ADNKSLGQFNLDGINPAPRGMPQIEVTFDIDADGILHVSAKDKNSGKEQKITIKASSGLN
EDEIQKMVRDAEANAEADRKFEELVQTRNQGDHLLHSTRKQVEEAGDKLPADDKTAIESA
LTALETALKGEDKAAIEAKMQELAQVSQKLMEIAQQQHA

Ligands and cofactors

IDNameFormulaCopies
A1DFXpeptide PA1-AC40 H55 N7 O71

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

Primary citation

Reengineering Protease Inhibitors to Disrupt Hsp70 Chaperone Function. Richards, A., Ariza-Mateos, A., Ghosh, A. et al. Angew Chem Int Ed Engl (2026) 65:e1777033-e1777033. DOI 10.1002/anie.1777033 · PubMed

Other PDB entries of the same protein (UniProt P0A6Y8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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