Crystal structure of an artificial dimeric DnaK complex. Determined by X-ray diffraction at 1.4 Å resolution. Released 17 Apr 2013.
Explore 4F01 in 3D Show helices and sheets RCSB PDB PDBe
4F01 contains 17 α-helices and 24 β-strands across 2 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 388-390 | 3 | 1 |
| β-strand | 394 | 1 | 2 |
| β-strand | 399-403 | 5 | 3 |
| β-strand | 407-412 | 6 | 3 |
| β-strand | 417 | 1 | 2 |
| β-strand | 420-428 | 9 | 1 |
| β-strand | 436-442 | 7 | 3 |
| β-strand | 447 | 1 | 3 |
| α-helix | 448-450 | 3 | |
| β-strand | 452-459 | 8 | 3 |
| α-helix | 462-464 | 3 | |
| β-strand | 472-478 | 7 | 1 |
| β-strand | 484-490 | 7 | 1 |
| β-strand | 496-500 | 5 | 1 |
| α-helix | 501-502 | 2 | |
| α-helix | 503-505 | 3 | |
| α-helix | 509-521 | 13 | |
| α-helix | 523-553 | 31 | |
| α-helix | 554-556 | 3 | |
| α-helix | 559-577 | 19 | |
| α-helix | 581-594 | 14 | |
| α-helix | 596-600 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 388-390 | 3 | 1 |
| β-strand | 394 | 1 | 4 |
| β-strand | 399-403 | 5 | 5 |
| β-strand | 407-412 | 6 | 5 |
| β-strand | 417 | 1 | 4 |
| β-strand | 420-428 | 9 | 1 |
| β-strand | 436-442 | 7 | 5 |
| β-strand | 447 | 1 | 5 |
| α-helix | 448-450 | 3 | |
| β-strand | 452-459 | 8 | 5 |
| α-helix | 462-464 | 3 | |
| β-strand | 472-478 | 7 | 1 |
| β-strand | 483-490 | 8 | 1 |
| β-strand | 496-502 | 7 | 1 |
| α-helix | 509-521 | 13 | |
| α-helix | 523-552 | 30 | |
| α-helix | 561-575 | 15 | |
| α-helix | 581-593 | 13 | |
| α-helix | 596-603 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Chaperone protein DnaK | A, B | protein | 241 | Escherichia coli | P0A6Y8 (AlphaFold model) |
>4F01_1 Chaperone protein DnaK (chains A, B) MGHHHHHHHHHHSSGHIEGRHMVLLLDVTPLSLGIETMGGVMTTLIAKNTTIPTKHSQVF STAEDNQSAVTIHVLQGERKRAADNKSLGQFNLDGINPAPRGMPQIEVTFDIDADGILHV SAKDKNSGKEQKITIKASSGLNEDEIQKMVRDAEANAEADRKFEELVQTRNQGDHLLHST RKQVEEAGDKLPADDKTAIESALTALETALKGEDKAAIEAKMQELAQVSQKLMEIAQQQH A
Structural Studies on the Forward and Reverse Binding Modes of Peptides to the Chaperone DnaK. Zahn, M., Berthold, N., Kieslich, B. et al. J Mol Biol (2013) 425:2463-2479. DOI 10.1016/j.jmb.2013.03.041 · PubMed
Other PDB entries of the same protein (UniProt P0A6Y8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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