4PSX: Histone acetyltransferase complex
Crystal structure of histone acetyltransferase complex. Determined by X-ray diffraction at 2.51 Å resolution. Released 9 Jul 2014.
- Method
- X-ray diffraction
- Resolution
- 2.51 Å
- Organisms
- Saccharomyces cerevisiae, Saccharomyces cerevisiae S288c
- Chains
- 8
- Atoms
- 12,392
- Mol. weight
- 180.3 kDa
- Ligands
- COA
- Released
- 9 Jul 2014
Explore 4PSX in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4PSX contains 47 α-helices and 91 β-strands across 8 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: 15 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-11 | 4 | |
| 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 | 83-88 | 6 | |
| 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 | |
| β-strand | 175-181 | 7 | 4 |
| β-strand | 187-197 | 11 | 4 |
| α-helix | 202-207 | 6 | |
| β-strand | 213-222 | 10 | 4 |
| α-helix | 224-226 | 3 | |
| α-helix | 231-244 | 14 | |
| β-strand | 249-254 | 6 | 4 |
| α-helix | 259-276 | 18 | |
| α-helix | 278-283 | 6 | |
| α-helix | 290-300 | 11 | |
| β-strand | 302 | 1 | 4 |
| α-helix | 304-317 | 14 | |
Chain B: 5 helices, 29 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-18 | 9 | |
| α-helix | 21-24 | 4 | |
| β-strand | 25-32 | 8 | 5 |
| β-strand | 40-42 | 3 | 6 |
| α-helix | 45-47 | 3 | |
| β-strand | 48-50 | 3 | 6 |
| β-strand | 54-61 | 8 | 6 |
| β-strand | 71-81 | 11 | 6 |
| α-helix | 82-84 | 3 | |
| β-strand | 109-117 | 9 | 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 | 165-168 | 4 | 8 |
| β-strand | 175-179 | 5 | 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 | 244-249 | 6 | 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 | |
| β-strand | 344-348 | 5 | 11 |
| β-strand | 355-360 | 6 | 5 |
| β-strand | 367-372 | 6 | 5 |
| β-strand | 376-382 | 7 | 5 |
Chains C and F: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 31-39 | 9 | |
Chain D: 16 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-11 | 4 | |
| β-strand | 12-14 | 3 | 12 |
| α-helix | 15-18 | 4 | |
| β-strand | 19-24 | 6 | 13 |
| β-strand | 28-31 | 4 | 13 |
| α-helix | 37-40 | 4 | |
| β-strand | 45-47 | 3 | 12 |
| β-strand | 49-50 | 2 | 14 |
| β-strand | 53-59 | 7 | 13 |
| β-strand | 65-70 | 6 | 13 |
| β-strand | 73-74 | 2 | 14 |
| α-helix | 83-88 | 6 | |
| β-strand | 97 | 1 | 13 |
| α-helix | 101-114 | 14 | |
| α-helix | 117-119 | 3 | |
| β-strand | 122-129 | 8 | 15 |
| β-strand | 132-140 | 9 | 15 |
| α-helix | 144-153 | 10 | |
| α-helix | 155-160 | 6 | |
| β-strand | 175-181 | 7 | 15 |
| β-strand | 187-197 | 11 | 15 |
| α-helix | 202-207 | 6 | |
| β-strand | 213-222 | 10 | 15 |
| α-helix | 224-226 | 3 | |
| α-helix | 231-245 | 15 | |
| β-strand | 249-254 | 6 | 15 |
| α-helix | 259-276 | 18 | |
| α-helix | 278-281 | 4 | |
| α-helix | 285-287 | 3 | |
| α-helix | 290-300 | 11 | |
| β-strand | 302 | 1 | 15 |
| α-helix | 304-317 | 14 | |
Chain E: 7 helices, 30 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-19 | 10 | |
| α-helix | 21-24 | 4 | |
| β-strand | 25-32 | 8 | 16 |
| β-strand | 40-42 | 3 | 17 |
| α-helix | 45-47 | 3 | |
| β-strand | 48-49 | 2 | 17 |
| α-helix | 50 | 1 | |
| β-strand | 54-61 | 8 | 17 |
| β-strand | 71-81 | 11 | 17 |
| α-helix | 82-85 | 4 | |
| β-strand | 109-117 | 9 | 17 |
| β-strand | 121-127 | 7 | 18 |
| β-strand | 130-138 | 9 | 18 |
| β-strand | 143-147 | 5 | 18 |
| β-strand | 151-156 | 6 | 18 |
| β-strand | 165-168 | 4 | 19 |
| β-strand | 175-179 | 5 | 19 |
| β-strand | 185-189 | 5 | 19 |
| β-strand | 201-203 | 3 | 19 |
| β-strand | 211-216 | 6 | 20 |
| β-strand | 223-228 | 6 | 20 |
| β-strand | 232-237 | 6 | 20 |
| β-strand | 244-249 | 6 | 20 |
| β-strand | 254-259 | 6 | 21 |
| β-strand | 266-271 | 6 | 21 |
| β-strand | 276-280 | 5 | 21 |
| β-strand | 283 | 1 | 21 |
| β-strand | 289-291 | 3 | 21 |
| β-strand | 298-303 | 6 | 22 |
| β-strand | 310-315 | 6 | 22 |
| β-strand | 320-324 | 5 | 22 |
| α-helix | 325-327 | 3 | |
| α-helix | 334-337 | 4 | |
| β-strand | 344-348 | 5 | 22 |
| β-strand | 355-360 | 6 | 16 |
| β-strand | 367-372 | 6 | 16 |
| β-strand | 376-382 | 7 | 16 |
Chains P and Y: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-7 | 4 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Histone acetyltransferase type B catalytic subunit | A, D | protein | 320 | Saccharomyces cerevisiae | Q12341 (AlphaFold model) |
| Histone acetyltransferase type B subunit 2 | B, E | protein | 401 | Saccharomyces cerevisiae | P39984 (AlphaFold model) |
| Histone H4 | C, F | protein | 48 | Saccharomyces cerevisiae | P02309 (AlphaFold model) |
| Histone H3 | P, Y | protein | 15 | Saccharomyces cerevisiae S288c | P61830 (AlphaFold model) |
Sequence of entity 1 (A, D), FASTA
>4PSX_1 Histone acetyltransferase type B catalytic subunit (chains A, D)
MSANDFKPETWTSSANEALRVSIVGENAVQFSPLFTYPIYGDSEKIYGYKDLIIHLAFDS
VTFKPYVNVKYSAKLGDDNIVDVEKKLLSFLPKDDVIVRDEAKWVDCFAEERKTHNLSDV
FEKVSEYSLNGEEFVVYKSSLVDDFARRMHRRVQIFSLLFIEAANYIDETDPSWQIYWLL
NKKTKELIGFVTTYKYWHYLGAKSFDEDIDKKFRAKISQFLIFPPYQNKGHGSCLYEAII
QSWLEDKSITEITVEDPNEAFDDLRDRNDIQRLRKLGYDAVFQKHSDLSDEFLESSRKSL
KLEERQFNRLVEMLLLLNNS
Sequence of entity 2 (B, E), FASTA
>4PSX_2 Histone acetyltransferase type B subunit 2 (chains B, E)
MENQEKPLSVDEEYDLWKSNVPLMYDFVSETRLTWPSLTVQWLPTPVQELDGGFIKQELI
IGTHTSGEEENYLKFAEINLPKEILSNEDPQEEAGEEYQSSLPAPRSNIRITAKYEHEEE
ITRARYMPQDPNIVATINGQGTTFLYSRSEGLQSTLKFHKDNGYALSFSTLVKGRLLSGS
DDHTVALWEVGSGGDPTKPVRTWNDLHSDIINDNKWHNFNKDLFGTVSEDSLLKINDVRA
NNTTIDTVKCPQPFNTLAFSHHSSNLLAAAGMDSYVYLYDLRNMKEPLHHMSGHEDAVNN
LEFSTHVDGVVVSSGSDNRLMMWDLKQIGAEQTPDDAEDGVPELIMVHAGHRSSVNDFDL
NPQIPWLVASAEEENILQVWKCSHSLPIVGGPPKVNKDIIS
Sequence of entity 3 (C, F), FASTA
>4PSX_3 Histone H4 (chains C, F)
SGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISG
Sequence of entity 4 (P, Y), FASTA
>4PSX_4 Histone H3 (chains P, Y)
ARTKQTARKSTGGKA
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| COA | Coenzyme a | C21 H36 N7 O16 P3 S | 2 |
Water and common crystallization additives (SO4) are not listed.
Primary citation
Hat2p recognizes the histone H3 tail to specify the acetylation of the newly synthesized H3/H4 heterodimer by the Hat1p/Hat2p complex. Li, Y., Zhang, L., Liu, T. et al. Genes Dev (2014) 28:1217-1227. DOI 10.1101/gad.240531.114 · PubMed
Other PDB entries of the same protein (UniProt Q12341 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 4PSW 2.1 Å, Crystal structure of histone acetyltransferase complex
- 1BOB 2.3 Å, Histone acetyltransferase HAT1 from saccharomyces cerevisiae in complex with acetyl…
- 7XAY 3.3 Å, Crystal structure of Hat1-Hat2-Asf1-H3-H4
Browse structure collections
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