Crystal structure of EBV tegument protein BNRF1 in complex with histone chaperone DAXX and histones H3.3-H4. Determined by X-ray diffraction at 3.5 Å resolution. Released 7 Sept 2016.
Explore 5KDM in 3D Show helices and sheets RCSB PDB PDBe
5KDM contains 25 α-helices and 19 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 |
|---|---|---|---|
| α-helix | 48-57 | 10 | |
| α-helix | 64-78 | 15 | |
| β-strand | 83-85 | 3 | 1 |
| α-helix | 86-109 | 24 | |
| β-strand | 119 | 1 | 2 |
| α-helix | 121-130 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 31-40 | 10 | |
| β-strand | 46 | 1 | 2 |
| α-helix | 50-75 | 26 | |
| β-strand | 80-81 | 2 | 1 |
| α-helix | 83-90 | 8 | |
| α-helix | 95-97 | 3 | |
| β-strand | 100 | 1 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 185-207 | 23 | |
| β-strand | 209-210 | 2 | 1 |
| α-helix | 212-216 | 5 | |
| α-helix | 221-242 | 22 | |
| α-helix | 267-272 | 6 | |
| α-helix | 286-298 | 13 | |
| α-helix | 306-334 | 29 | |
| α-helix | 339-342 | 4 | |
| α-helix | 350-352 | 3 | |
| α-helix | 355-383 | 29 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 393-397 | 5 | 4 |
| α-helix | 415-433 | 19 | |
| β-strand | 439 | 1 | 4 |
| β-strand | 443 | 1 | 4 |
| β-strand | 450 | 1 | 5 |
| α-helix | 451-456 | 6 | |
| β-strand | 463-467 | 5 | 4 |
| α-helix | 473-476 | 4 | |
| α-helix | 491-500 | 10 | |
| α-helix | 503 | 1 | |
| β-strand | 504 | 1 | 5 |
| α-helix | 505 | 1 | |
| β-strand | 508-512 | 5 | 4 |
| β-strand | 519 | 1 | 6 |
| β-strand | 522 | 1 | 6 |
| α-helix | 524-534 | 11 | |
| β-strand | 539-546 | 8 | 4 |
| β-strand | 548 | 1 | 3 |
| β-strand | 551-554 | 4 | 4 |
| α-helix | 560-562 | 3 | |
| β-strand | 575-576 | 2 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone H3.3 | A | protein | 135 | Homo sapiens | P84243 (AlphaFold model) |
| Histone H4 | B | protein | 102 | Homo sapiens | P62805 (AlphaFold model) |
| Death domain-associated protein 6 | C | protein | 212 | Homo sapiens | Q9UER7 (AlphaFold model) |
| Major tegument protein | D | protein | 219 | Epstein-Barr virus (strain AG876) | Q1HVJ0 |
>5KDM_1 Histone H3.3 (chains A) ARTKQTARKSTGGKAPRKQLATKAARKSAPSTGGVKKPHRYRPGTVALREIRRYQKSTEL LIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIM PKDIQLARRIRGERA
>5KDM_2 Histone H4 (chains B) SGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKV FLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
>5KDM_3 Death domain-associated protein 6 (chains C) SPRTRGSRRQIQRLEQLLALYVAEIRRLQEKELDLSELDDPDSAYLQEARLKRKLIRLFG RLCELKDCSSLTGRVIEQRIPYRGTRYPEVNRRIERLINKPGPDTFPDYGDVLRAVEKAA ARHSLGLPRQQLQLMAQDAFRDVGIRLQERRHLDLIYNFGCHLTDDYRPGVDPALSDPVL ARRLRENRSLAMSRLDEVISKYAMLQDKSEEG
>5KDM_4 Major tegument protein (chains D) QALDTVRYDYGHYLIMLGPFQPWSGLTAPPCPYAESSWAQAAVQTALELFSALYPAPCIS GYARPPGPSAVIEHLGSLVPKGGLLLFLSHLPDDVKDGLGEMGPARATGPGMQQFVSSYF LNPACSNVFITVRQRGEKINGRTVLQALGRACDMAGCQHYVLGSTVPLGGLNFVNDLASP VSTAEMMDDFSPFFTVEFPPIQEEGASSPVPLDVDESMD
Structural basis underlying viral hijacking of a histone chaperone complex. Huang, H., Deng, Z., Vladimirova, O. et al. Nat Commun (2016) 7:12707-12707. DOI 10.1038/ncomms12707 · PubMed
Other PDB entries of the same protein (UniProt P84243 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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