Crystal structure of the substrate binding domain of E.coli DnaK in complex with PR-bombesin in space group P21212. Determined by X-ray diffraction at 2.1 Å resolution. Released 24 Apr 2013.
Explore 4EZV in 3D Show helices and sheets RCSB PDB PDBe
4EZV contains 18 α-helices and 24 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 | 1 | 1 |
| β-strand | 399-403 | 5 | 2 |
| β-strand | 407-412 | 6 | 2 |
| α-helix | 416 | 1 | |
| β-strand | 417 | 1 | 1 |
| β-strand | 420-428 | 9 | 3 |
| β-strand | 435-442 | 8 | 2 |
| β-strand | 447 | 1 | 2 |
| α-helix | 448-450 | 3 | |
| β-strand | 452-460 | 9 | 2 |
| α-helix | 462-463 | 2 | |
| 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 | 523-553 | 31 | |
| α-helix | 554-556 | 3 | |
| α-helix | 559-576 | 18 | |
| α-helix | 581-593 | 13 | |
| α-helix | 596-606 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| 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 | 6 |
| 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 | 6 |
| β-strand | 484-490 | 7 | 6 |
| β-strand | 496-501 | 6 | 6 |
| 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 | 596-603 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-8 | 3 | |
| β-strand | 12-14 | 3 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-14 | 3 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Chaperone protein DnaK | A, B | protein | 219 | Escherichia coli | P0A6Y8 (AlphaFold model) |
| Proline rich bombesin-related protein | C, D | protein | 17 | Bombina maxima | Q8QFP2 (AlphaFold model) |
>4EZV_1 Chaperone protein DnaK (chains A, B) VLLLDVTPLSLGIETMGGVMTTLIAKNTTIPTKHSQVFSTAEDNQSAVTIHVLQGERKRA ADNKSLGQFNLDGINPAPRGMPQIEVTFDIDADGILHVSAKDKNSGKEQKITIKASSGLN EDEIQKMVRDAEANAEADRKFEELVQTRNQGDHLLHSTRKQVEEAGDKLPADDKTAIESA LTALETALKGEDKAAIEAKMQELAQVSQKLMEIAQQQHA
>4EZV_2 Proline rich bombesin-related protein (chains C, D) EKKPPRPPQWAVGHFMM
Structural studies of DnaK in complex with proline rich antimicrobial peptides reveal two different peptide binding modes. Zahn, M., Straeter, N. To be published.
Other PDB entries of the same protein (UniProt P0A6Y8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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