Crystal structure of the substrate binding domain of E.coli DnaK in complex with PR-39 (residues 1 to 15). Determined by X-ray diffraction at 1.9 Å resolution. Released 17 Apr 2013.
Explore 4EZO in 3D Show helices and sheets RCSB PDB PDBe
4EZO contains 18 α-helices and 26 β-strands across 4 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 | 394-395 | 2 | 1 |
| β-strand | 399-403 | 5 | 2 |
| β-strand | 407-412 | 6 | 2 |
| β-strand | 416-417 | 2 | 1 |
| β-strand | 420-426 | 7 | 3 |
| β-strand | 427 | 1 | 4 |
| β-strand | 436-442 | 7 | 2 |
| β-strand | 447 | 1 | 2 |
| α-helix | 448-450 | 3 | |
| β-strand | 452-459 | 8 | 2 |
| α-helix | 462-464 | 3 | |
| β-strand | 472-478 | 7 | 3 |
| β-strand | 484-490 | 7 | 3 |
| β-strand | 496-501 | 6 | 3 |
| α-helix | 509-521 | 13 | |
| α-helix | 523-550 | 28 | |
| α-helix | 554-556 | 3 | |
| α-helix | 559-577 | 19 | |
| α-helix | 581-594 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 394 | 1 | 5 |
| β-strand | 399-403 | 5 | 6 |
| β-strand | 407-412 | 6 | 6 |
| α-helix | 416 | 1 | |
| β-strand | 417 | 1 | 5 |
| β-strand | 420-426 | 7 | 7 |
| β-strand | 427-428 | 2 | 8 |
| β-strand | 435-442 | 8 | 6 |
| β-strand | 447 | 1 | 6 |
| α-helix | 448-450 | 3 | |
| β-strand | 452-460 | 9 | 6 |
| α-helix | 462-464 | 3 | |
| β-strand | 472-478 | 7 | 7 |
| β-strand | 484-490 | 7 | 7 |
| β-strand | 496-501 | 6 | 7 |
| α-helix | 509-521 | 13 | |
| α-helix | 523-553 | 31 | |
| α-helix | 554-556 | 3 | |
| α-helix | 559-576 | 18 | |
| α-helix | 581-593 | 13 | |
| α-helix | 596-602 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8 | 1 | 4 |
| α-helix | 9-11 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-9 | 2 | 8 |
| α-helix | 10-12 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Chaperone protein DnaK | A, B | protein | 219 | Escherichia coli | P0A6Y8 (AlphaFold model) |
| Antibacterial protein PR-39 | C, D | protein | 15 | Sus scrofa | P80054 (AlphaFold model) |
>4EZO_1 Chaperone protein DnaK (chains A, B) VLLLDVTPLSLGIETMGGVMTTLIAKNTTIPTKHSQVFSTAEDNQSAVTIHVLQGERKRA ADNKSLGQFNLDGINPAPRGMPQIEVTFDIDADGILHVSAKDKNSGKEQKITIKASSGLN EDEIQKMVRDAEANAEADRKFEELVQTRNQGDHLLHSTRKQVEEAGDKLPADDKTAIESA LTALETALKGEDKAAIEAKMQELAQVSQKLMEIAQQQHA
>4EZO_2 Antibacterial protein PR-39 (chains C, D) RRRPRPPYLPRPRPP
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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