Crystal structure of Rtt109-Asf1-H3-H4 complex. Determined by X-ray diffraction at 3.6 Å resolution. Released 25 Jul 2018.
Explore 5ZBB in 3D Show helices and sheets RCSB PDB PDBe
5ZBB contains 29 α-helices and 30 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 | 8-15 | 8 | |
| β-strand | 17 | 1 | 1 |
| β-strand | 21-29 | 9 | 2 |
| β-strand | 32-34 | 3 | 2 |
| α-helix | 39-41 | 3 | |
| α-helix | 45-48 | 4 | |
| β-strand | 49-60 | 12 | 2 |
| β-strand | 70-82 | 13 | 2 |
| β-strand | 85-95 | 11 | 2 |
| α-helix | 98-101 | 4 | |
| α-helix | 110-126 | 17 | |
| β-strand | 132-140 | 9 | 2 |
| α-helix | 150-152 | 3 | |
| α-helix | 161-177 | 17 | |
| β-strand | 180 | 1 | 2 |
| β-strand | 201-207 | 7 | 2 |
| α-helix | 213-216 | 4 | |
| α-helix | 217-219 | 3 | |
| α-helix | 222-226 | 5 | |
| β-strand | 234-235 | 2 | 2 |
| α-helix | 251-254 | 4 | |
| α-helix | 262-271 | 10 | |
| α-helix | 296-303 | 8 | |
| β-strand | 315-323 | 9 | 2 |
| β-strand | 415-418 | 4 | 2 |
| α-helix | 420-431 | 12 | |
| α-helix | 438-455 | 18 | |
| β-strand | 463-466 | 4 | 2 |
| β-strand | 469 | 1 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-11 | 8 | 3 |
| β-strand | 16-17 | 2 | 4 |
| α-helix | 21 | 1 | |
| β-strand | 22-30 | 9 | 3 |
| β-strand | 38-45 | 8 | 4 |
| β-strand | 54-62 | 9 | 4 |
| β-strand | 68-76 | 9 | 3 |
| α-helix | 77-80 | 4 | |
| α-helix | 81-83 | 3 | |
| β-strand | 92-101 | 10 | 4 |
| β-strand | 104-117 | 14 | 4 |
| α-helix | 120-124 | 5 | |
| α-helix | 132-134 | 3 | |
| β-strand | 135-139 | 5 | 4 |
| β-strand | 145-148 | 4 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 46-47 | 2 | 5 |
| α-helix | 48-50 | 3 | |
| α-helix | 64-77 | 14 | |
| β-strand | 83-84 | 2 | 6 |
| α-helix | 86-113 | 28 | |
| β-strand | 118-119 | 2 | 5 |
| α-helix | 121-131 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 25-28 | 4 | |
| α-helix | 31-40 | 10 | |
| β-strand | 45-46 | 2 | 5 |
| α-helix | 48-50 | 3 | |
| α-helix | 51-75 | 25 | |
| β-strand | 80-81 | 2 | 6 |
| α-helix | 83-91 | 9 | |
| β-strand | 95-98 | 4 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA damage response protein Rtt109, putative | A | protein | 544 | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) | Q4WUS9 (AlphaFold model) |
| Histone chaperone asf1 | B | protein | 188 | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) | Q4WXX5 (AlphaFold model) |
| Histone H3 | C | protein | 136 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P61830 (AlphaFold model) |
| Histone H4 | D | protein | 103 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P02309 (AlphaFold model) |
>5ZBB_1 DNA damage response protein Rtt109, putative (chains A) SMSKVDVDLGDSLAKVLPTGVKVTIRHISSAPSPCVALFAAPPGEEPESTFCENHFLAVS ISPNENEESEVIIFGIEVLVYGTAHLTTIFVSKADSTGYLHLLKNAPKVSLLRLISNAFL SFLVQTHQRPGVRLMVSLFARAQNQYLFPGSIENPEKHVLDDRGLIKWWCRVIDPILREY EPETGSHEKAVDDQTQESAKSSATAFLIVPGCDKFETRGFFPITARSDGKDRPRWLNSYP LHQLCDNPNAPPRCLVPRFPDDPKTRFLIDLDDELPESTGAAGSKENSGHWRSVKSLAQF WEMMSFRQECSAGRLVGFLWLVINPPGLVNSVQMTSSRVASRDVENVLSESAKTTHDATK QKDEAASVSSPPHPSTSGLQTSPIALPGVSSSDTHATVQQATGPSAFFWPDTGRGHAVLS EEDYKAAINFLIDQDFNTKHKAIASTKAWAEKVASLADQLWVGQRVEGRNATTEPGQKHT DATTVINTAFVRKRKTADEESDKPGEVRGAPGDSEEVNPTPVQSNQAPSVNVLNANLLRK KKKT
>5ZBB_2 Histone chaperone asf1 (chains B) MGSSHHHHHHSSGLVPRGSHMASMTGGQQMGRGSMSVVSLLGVKIVNNPAPFLAPYQFEI TFECLEQLQKDLEWKLTYVGSATSSEYDQELDSLLVGPIPVGVNKFLFEADAPDLKRIPT SEILGVTVILLTCSYDGREFVRVGYYVNNEYDSEELTQDPPAKPIIERIRRNILAEKPRV TRFAIKWD
>5ZBB_3 Histone H3 (chains C) MARTKQTARKSTGGKAPRKQLASKAARKSAPSTGGVKKPHRYKPGTVALREIRRFQKSTE LLIRKLPFQRLVREIAQDFKTDLRFQSSAIGALQESVEAYLVSLFEDTNLAAIHAKRVTI QKKDIKLARRLRGERS
>5ZBB_4 Histone H4 (chains D) MSGRGKGGKGLGKGGAKRHRKILRDNIQGITKPAIRRLARRGGVKRISGLIYEEVRAVLK SFLESVIRDSVTYTEHAKRKTVTSLDVVYALKRQGRTLYGFGG
Multisite Substrate Recognition in Asf1-Dependent Acetylation of Histone H3 K56 by Rtt109. Zhang, L., Serra-Cardona, A., Zhou, H. et al. Cell (2018) 174:818-830.e11. DOI 10.1016/j.cell.2018.07.005 · PubMed
Other PDB entries of the same protein (UniProt Q4WUS9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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