Crystal structure of Rtt109 from Aspergillus fumigatus. Determined by X-ray diffraction at 2.5 Å resolution. Released 25 Jul 2018.
Explore 5ZB9 in 3D Show helices and sheets RCSB PDB PDBe
5ZB9 contains 17 α-helices and 16 β-strands across 1 chain. 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 | |
| β-strand | 44 | 1 | 3 |
| α-helix | 45-48 | 4 | |
| β-strand | 49-60 | 12 | 2 |
| β-strand | 70-81 | 12 | 2 |
| β-strand | 85-95 | 11 | 2 |
| α-helix | 99-101 | 3 | |
| α-helix | 110-126 | 17 | |
| β-strand | 132-139 | 8 | 2 |
| α-helix | 150-152 | 3 | |
| α-helix | 161-176 | 16 | |
| β-strand | 180 | 1 | 2 |
| α-helix | 192-197 | 6 | |
| β-strand | 201-207 | 7 | 2 |
| α-helix | 213-217 | 5 | |
| α-helix | 222-226 | 5 | |
| β-strand | 234-235 | 2 | 2 |
| α-helix | 240-243 | 4 | |
| α-helix | 251-253 | 3 | |
| α-helix | 262-271 | 10 | |
| α-helix | 296-303 | 8 | |
| α-helix | 307-309 | 3 | |
| β-strand | 316-323 | 8 | 2 |
| β-strand | 339 | 1 | 3 |
| β-strand | 416-418 | 3 | 2 |
| α-helix | 420-431 | 12 | |
| α-helix | 438-456 | 19 | |
| β-strand | 463-466 | 4 | 2 |
| β-strand | 469 | 1 | 1 |
| 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) |
>5ZB9_1 DNA damage response protein Rtt109, putative (chains A) SMSKVDVDLGDSLAKVLPTGVKVTIRHISSAPSPCVALFAAPPGEEPESTFCENHFLAVS ISPNENEESEVIIFGIEVLVYGTAHLTTIFVSKADSTGYLHLLKNAPKVSLLRLISNAFL SFLVQTHQRPGVRLMVSLFARAQNQYLFPGSIENPEKHVLDDRGLIKWWCRVIDPILREY EPETGSHEKAVDDQTQESAKSSATAFLIVPGCDKFETRGFFPITARSDGKDRPRWLNSYP LHQLCDNPNAPPRCLVPRFPDDPKTRFLIDLDDELPESTGAAGSKENSGHWRSVKSLAQF WEMMSFRQECSAGRLVGFLWLVINPPGLVNSVQMTSSRVASRDVENVLSESAKTTHDATK QKDEAASVSSPPHPSTSGLQTSPIALPGVSSSDTHATVQQATGPSAFFWPDTGRGHAVLS EEDYKAAINFLIDQDFNTKHKAIASTKAWAEKVASLADQLWVGQRVEGRNATTEPGQKHT DATTVINTAFVRKRKTADEESDKPGEVRGAPGDSEEVNPTPVQSNQAPSVNVLNANLLRK KKKT
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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