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

ElementResiduesLengthSheet
α-helix8-114
β-strand12-1431
α-helix15-184
β-strand19-2462
β-strand28-3142
α-helix37-404
β-strand45-4731
β-strand49-5023
β-strand53-5972
β-strand65-7062
β-strand73-7423
α-helix83-886
β-strand97-9822
α-helix101-11414
α-helix117-1193
β-strand122-12984
β-strand132-14094
α-helix144-15310
α-helix155-1606
β-strand175-18174
β-strand187-197114
α-helix202-2076
β-strand213-222104
α-helix224-2263
α-helix231-24414
β-strand249-25464
α-helix259-27618
α-helix278-2836
α-helix290-30011
β-strand30214
α-helix304-31714
Chain B: 5 helices, 29 β-strands
ElementResiduesLengthSheet
α-helix10-189
α-helix21-244
β-strand25-3285
β-strand40-4236
α-helix45-473
β-strand48-5036
β-strand54-6186
β-strand71-81116
α-helix82-843
β-strand109-11796
β-strand121-12777
β-strand130-13897
β-strand143-14757
β-strand151-15667
β-strand165-16848
β-strand175-17958
β-strand185-18958
β-strand201-20338
β-strand211-21669
β-strand223-22869
β-strand232-23769
β-strand244-24969
β-strand254-259610
β-strand266-271610
β-strand276-280510
β-strand289-291310
β-strand298-303611
β-strand310-315611
β-strand320-324511
α-helix325-3273
β-strand344-348511
β-strand355-36065
β-strand367-37265
β-strand376-38275
Chains C and F: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix31-399
Chain D: 16 helices, 16 β-strands
ElementResiduesLengthSheet
α-helix8-114
β-strand12-14312
α-helix15-184
β-strand19-24613
β-strand28-31413
α-helix37-404
β-strand45-47312
β-strand49-50214
β-strand53-59713
β-strand65-70613
β-strand73-74214
α-helix83-886
β-strand97113
α-helix101-11414
α-helix117-1193
β-strand122-129815
β-strand132-140915
α-helix144-15310
α-helix155-1606
β-strand175-181715
β-strand187-1971115
α-helix202-2076
β-strand213-2221015
α-helix224-2263
α-helix231-24515
β-strand249-254615
α-helix259-27618
α-helix278-2814
α-helix285-2873
α-helix290-30011
β-strand302115
α-helix304-31714
Chain E: 7 helices, 30 β-strands
ElementResiduesLengthSheet
α-helix10-1910
α-helix21-244
β-strand25-32816
β-strand40-42317
α-helix45-473
β-strand48-49217
α-helix501
β-strand54-61817
β-strand71-811117
α-helix82-854
β-strand109-117917
β-strand121-127718
β-strand130-138918
β-strand143-147518
β-strand151-156618
β-strand165-168419
β-strand175-179519
β-strand185-189519
β-strand201-203319
β-strand211-216620
β-strand223-228620
β-strand232-237620
β-strand244-249620
β-strand254-259621
β-strand266-271621
β-strand276-280521
β-strand283121
β-strand289-291321
β-strand298-303622
β-strand310-315622
β-strand320-324522
α-helix325-3273
α-helix334-3374
β-strand344-348522
β-strand355-360616
β-strand367-372616
β-strand376-382716
Chains P and Y: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix4-74

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Histone acetyltransferase type B catalytic subunitA, Dprotein320Saccharomyces cerevisiaeQ12341 (AlphaFold model)
Histone acetyltransferase type B subunit 2B, Eprotein401Saccharomyces cerevisiaeP39984 (AlphaFold model)
Histone H4C, Fprotein48Saccharomyces cerevisiaeP02309 (AlphaFold model)
Histone H3P, Yprotein15Saccharomyces cerevisiae S288cP61830 (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

IDNameFormulaCopies
COACoenzyme aC21 H36 N7 O16 P3 S2

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:

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