7XAY: Hat1-Hat2-Asf1-H3-H4
Crystal structure of Hat1-Hat2-Asf1-H3-H4. Determined by X-ray diffraction at 3.3 Å resolution. Released 18 May 2022.
- Method
- X-ray diffraction
- Resolution
- 3.3 Å
- Organisms
- Saccharomyces cerevisiae S288C, Aspergillus fumigatus Af293
- Chains
- 5
- Atoms
- 8,267
- Mol. weight
- 137.61 kDa
- Ligands
- COA
- Released
- 18 May 2022
Explore 7XAY in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
7XAY contains 36 α-helices and 61 β-strands across 5 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.
Chain A: 17 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 12-14 | 3 | 1 |
| α-helix | 15-18 | 4 | |
| β-strand | 19-24 | 6 | 2 |
| β-strand | 28-31 | 4 | 2 |
| α-helix | 37-40 | 4 | |
| β-strand | 45-47 | 3 | 1 |
| β-strand | 49-50 | 2 | 3 |
| β-strand | 53-59 | 7 | 2 |
| β-strand | 65-70 | 6 | 2 |
| β-strand | 73-74 | 2 | 3 |
| α-helix | 83-90 | 8 | |
| α-helix | 92 | 1 | |
| β-strand | 97-98 | 2 | 2 |
| α-helix | 101-114 | 14 | |
| α-helix | 117-119 | 3 | |
| β-strand | 122-129 | 8 | 4 |
| β-strand | 132-140 | 9 | 4 |
| α-helix | 144-153 | 10 | |
| α-helix | 155-160 | 6 | |
| α-helix | 166-168 | 3 | |
| β-strand | 174-181 | 8 | 4 |
| β-strand | 187-197 | 11 | 4 |
| α-helix | 202-207 | 6 | |
| α-helix | 211-212 | 2 | |
| β-strand | 213-222 | 10 | 4 |
| α-helix | 224-226 | 3 | |
| α-helix | 231-245 | 15 | |
| β-strand | 249-254 | 6 | 4 |
| α-helix | 259-275 | 17 | |
| α-helix | 278-284 | 7 | |
| α-helix | 290-300 | 11 | |
| β-strand | 302 | 1 | 4 |
| α-helix | 304-314 | 11 | |
Chain B: 4 helices, 29 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-24 | 15 | |
| β-strand | 25-32 | 8 | 5 |
| β-strand | 40-42 | 3 | 6 |
| β-strand | 48-49 | 2 | 6 |
| β-strand | 54-61 | 8 | 6 |
| β-strand | 71-81 | 11 | 6 |
| α-helix | 82-85 | 4 | |
| β-strand | 110-117 | 8 | 6 |
| β-strand | 121-127 | 7 | 7 |
| β-strand | 130-138 | 9 | 7 |
| β-strand | 143-147 | 5 | 7 |
| β-strand | 151-156 | 6 | 7 |
| β-strand | 163-168 | 6 | 8 |
| β-strand | 175-180 | 6 | 8 |
| β-strand | 185-189 | 5 | 8 |
| β-strand | 201-203 | 3 | 8 |
| β-strand | 211-216 | 6 | 9 |
| β-strand | 223-228 | 6 | 9 |
| β-strand | 232-237 | 6 | 9 |
| β-strand | 246-249 | 4 | 9 |
| β-strand | 254-259 | 6 | 10 |
| β-strand | 266-271 | 6 | 10 |
| β-strand | 276-280 | 5 | 10 |
| β-strand | 289-291 | 3 | 10 |
| β-strand | 298-303 | 6 | 11 |
| β-strand | 310-315 | 6 | 11 |
| β-strand | 320-324 | 5 | 11 |
| α-helix | 325-327 | 3 | |
| α-helix | 334-337 | 4 | |
| β-strand | 344-348 | 5 | 11 |
| β-strand | 355-360 | 6 | 5 |
| β-strand | 367-372 | 6 | 5 |
| β-strand | 376-382 | 7 | 5 |
Chain C: 7 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-11 | 8 | 12 |
| β-strand | 16-17 | 2 | 13 |
| α-helix | 21 | 1 | |
| β-strand | 22-30 | 9 | 12 |
| β-strand | 38-45 | 8 | 13 |
| β-strand | 54-56 | 3 | 13 |
| β-strand | 60-62 | 3 | 13 |
| α-helix | 65-66 | 2 | |
| β-strand | 68-76 | 9 | 12 |
| α-helix | 77-79 | 3 | |
| α-helix | 81-83 | 3 | |
| α-helix | 86-88 | 3 | |
| β-strand | 91-101 | 11 | 13 |
| β-strand | 104-117 | 14 | 13 |
| α-helix | 120-124 | 5 | |
| α-helix | 132-134 | 3 | |
| β-strand | 135-148 | 14 | 13 |
Chain D: 4 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-7 | 4 | |
| β-strand | 54-56 | 3 | 5 |
| α-helix | 64-76 | 13 | |
| β-strand | 83-84 | 2 | 14 |
| α-helix | 86-113 | 28 | |
| β-strand | 118-119 | 2 | 15 |
| α-helix | 121-130 | 10 | |
Chain E: 4 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 26-28 | 3 | |
| α-helix | 31-39 | 9 | |
| β-strand | 45-46 | 2 | 15 |
| α-helix | 51-75 | 25 | |
| β-strand | 80-81 | 2 | 14 |
| α-helix | 83-91 | 9 | |
| β-strand | 95-98 | 4 | 13 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Soluble cytochrome b562,Histone acetyltransferase type B catalytic subunit | A | protein | 416 | Saccharomyces cerevisiae S288C | P0ABE7 (AlphaFold model), Q12341 (AlphaFold model) |
| Histone acetyltransferase type B subunit 2 | B | protein | 401 | Saccharomyces cerevisiae S288C | P39984 (AlphaFold model) |
| Histone chaperone asf1 | C | protein | 154 | Aspergillus fumigatus Af293 | Q4WXX5 (AlphaFold model) |
| Histone H3 | D | protein | 135 | Saccharomyces cerevisiae S288C | P61830 |
| Histone H4 | E | protein | 96 | Saccharomyces cerevisiae S288C | P02309 |
Sequence of entity 1 (A), FASTA
>7XAY_1 Soluble cytochrome b562,Histone acetyltransferase type B catalytic subunit (chains A)
ADLEDNWETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKD
FRHGFDILVGQIDDALKLANEGKVKEAQAAAEQLKTTRNAYIQKYLWTSSANEALRVSIV
GENAVQFSPLFTYPIYGDSEKIYGYKDLIIHLAFDSVTFKPYVNVKYSAKLGDDNIVDVE
KKLLSFLPKDDVIVRDEAKWVDCFAEERKTHNLSDVFEKVSEYSLNGEEFVVYKSSLVDD
FARRMHRRVQIFSLLFIEAANYIDETDPSWQIYWLLNKKTKELIGFVTTYKYWHYLGAKS
FDEDIDKKFRAKISQFLIFPPYQNKGHGSCLYEAIIQSWLEDKSITEITVEDPNEAFDDL
RDRNDIQRLRKLGYDAVFQKHSDLSDEFLESSRKSLKLEERQFNRLVEMLLLLNNS
Sequence of entity 2 (B), FASTA
>7XAY_2 Histone acetyltransferase type B subunit 2 (chains B)
MENQEKPLSVDEEYDLWKSNVPLMYDFVSETRLTWPSLTVQWLPTPVQELDGGFIKQELI
IGTHTSGEEENYLKFAEINLPKEILSNEDPQEEAGEEYQSSLPAPRSNIRITAKYEHEEE
ITRARYMPQDPNIVATINGQGTVFLYSRSEGLQSTLKFHKDNGYALSFSTLVKGRLLSGS
DDHTVALWEVGSGGDPTKPVRTWNDLHSDIINDNKWHNFNKDLFGTVSEDSLLKINDVRA
NNTTIDTVKCPQPFNTLAFSHHSSNLLAAAGMDSYVYLYDLRNMKEPLHHMSGHEDAVNN
LEFSTHVDGVVVSSGSDNRLMMWDLKQIGAEQTPDDAEDGVPELIMVHAGHRSSVNDFDL
NPQIPWLVASAEEENILQVWKCSHSLPIVGGPPKVNKDIIS
Sequence of entity 3 (C), FASTA
>7XAY_3 Histone chaperone asf1 (chains C)
MSVVSLLGVKIVNNPAPFLAPYQFEITFECLEQLQKDLEWKLTYVGSATSSEYDQELDSL
LVGPIPVGVNKFLFEADAPDLKRIPTSEILGVTVILLTCSYDGREFVRVGYYVNNEYDSE
ELTQDPPAKPIIERIRRNILAEKPRVTRFAIKWD
Sequence of entity 4 (D), FASTA
>7XAY_4 Histone H3 (chains D)
ARTKQTARKSTGGKAPRKQLASKAARKSAPSTGGVKKPHRYKPGTVALREIRRFQKSTEL
LIRKLPFQRLVREIAQDFKTDLRFQSSAIGALQESVEAYLVSLFEDTNLAAIHAKRVTIQ
KKDIKLARRLRGERS
Sequence of entity 5 (E), FASTA
>7XAY_5 Histone H4 (chains E)
GKGLGKGGAKRHRKILRDNIQGITKPAIRRLARRGGVKRISGLIYEEVRAVLKSFLESVI
RDSVTYTEHAKRKTVTSLDVVYALKRQGRTLYGFGG
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| COA | Coenzyme a | C21 H36 N7 O16 P3 S | 1 |
Primary citation
Topography of histone H3-H4 interaction with the Hat1-Hat2 acetyltransferase complex. Yue, Y., Yang, W.S., Zhang, L. et al. Genes Dev (2022) 36:408-413. DOI 10.1101/gad.349099.121 · PubMed
Other PDB entries of the same protein (UniProt P0ABE7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6DYF 1.1 Å, Cu(II)-bound structure of the engineered cyt cb562 variant, CH3Y
- 5YO6 1.2 Å, Crystal Structure of B562RIL with engineered disulfide bond T9C-A36C
- 4JEA 1.22 Å, Crystal structure of an engineered Zn-RIDC1 construct with four interfacial disulfide…
- 7LSJ 1.26 Å, Cu-bound crystal structure of the engineered cyt cb562 variant, DiCyt2 - H63A,…
- 7MK4 1.27 Å, Co-bound crystal structure of the engineered cyt cb562 variant, DiCyt2
- 6DYC 1.33 Å, Co(II)-bound structure of the engineered cyt cb562 variant, CH3
- 5YO4 1.37 Å, Crystal Structure of B562RIL with engineered disulfide bond K27C-A79C
- 256B 1.4 Å, Improvement of the 2.5 Å resolution model of cytochrome B562 by redetermining the…
- 6OT4 1.4 Å, Bimetallic dodecameric cage design 2 (BMC2) from cytochrome cb562
- 7LRV 1.4 Å, Ni-bound crystal structure of the engineered cyt cb562 variant, DiCyt2, crystallized in…
- 9PQ4 1.48 Å, Bi-bound structure of the H77C variant of TriCyt2
- 6DYG 1.49 Å, Fe(II)-bound structure of the engineered cyt cb562 variant, CH3Y
Browse structure collections
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