4PSW: Histone acetyltransferase complex

Name: PDB 4PSW: Crystal structure of histone acetyltransferase complex
Published: 2014-07-09
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transferase

Crystal structure of histone acetyltransferase complex. Determined by X-ray diffraction at 2.1 Å resolution. Released 9 Jul 2014.

Method: X-ray diffraction
Resolution: 2.1 Å
Organisms: Saccharomyces cerevisiae, Ophiophagus hannah
Chains: 3
Atoms: 6,398
Mol. weight: 87.37 kDa
Ligands: COA
Released: 9 Jul 2014

Explore 4PSW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4PSW contains 22 α-helices and 45 β-strands across 3 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	101-113	13
α-helix	117-120	4
β-strand	122-128	7	4
β-strand	133-140	8	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	259-275	17
α-helix	278-281	4
α-helix	290-300	11
β-strand	302	1	4
α-helix	304-318	15

Chain B: 6 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
α-helix	45-47	3
β-strand	48-49	2	6
α-helix	50	1
β-strand	54-62	9	6
β-strand	71-81	11	6
α-helix	82-85	4
β-strand	108-117	10	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
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: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	33-42	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone acetyltransferase type B catalytic subunit	A	protein	317	Saccharomyces cerevisiae	Q12341 (AlphaFold model)
Histone acetyltransferase type B subunit 2	B	protein	401	Saccharomyces cerevisiae	P39984 (AlphaFold model)
Histone H4 type VIII	C	protein	38	Ophiophagus hannah	V8PGJ1 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4PSW_1 Histone acetyltransferase type B catalytic subunit (chains A)
NDFKPETWTSSANEALRVSIVGENAVQFSPLFTYPIYGDSEKIYGYKDLIIHLAFDSVTF
KPYVNVKYSAKLGDDNIVDVEKKLLSFLPKDDVIVRDEAKWVDCFAEERKTHNLSDVFEK
VSEYSLNGEEFVVYKSSLVDDFARRMHRRVQIFSLLFIEAANYIDETDPSWQIYWLLNKK
TKELIGFVTTYKYWHYLGAKSFDEDIDKKFRAKISQFLIFPPYQNKGHGSCLYEAIIQSW
LEDKSITEITVEDPNEAFDDLRDRNDIQRLRKLGYDAVFQKHSDLSDEFLESSRKSLKLE
ERQFNRLVEMLLLLNNS

Sequence of entity 2 (B), FASTA

>4PSW_2 Histone acetyltransferase type B subunit 2 (chains B)
MENQEKPLSVDEEYDLWKSNVPLMYDFVSETRLTWPSLTVQWLPTPVQELDGGFIKQELI
IGTHTSGEEENYLKFAEINLPKEILSNEDPQEEAGEEYQSSLPAPRSNIRITAKYEHEEE
ITRARYMPQDPNIVATINGQGTTFLYSRSEGLQSTLKFHKDNGYALSFSTLVKGRLLSGS
DDHTVALWEVGSGGDPTKPVRTWNDLHSDIINDNKWHNFNKDLFGTVSEDSLLKINDVRA
NNTTIDTVKCPQPFNTLAFSHHSSNLLAAAGMDSYVYLYDLRNMKEPLHHMSGHEDAVNN
LEFSTHVDGVVVSSGSDNRLMMWDLKQIGAEQTPDDAEDGVPELIMVHAGHRSSVNDFDL
NPQIPWLVASAEEENILQVWKCSHSLPIVGGPPKVNKDIIS

Sequence of entity 3 (C), FASTA

>4PSW_3 Histone H4 type VIII (chains C)
GKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVK

Ligands and cofactors

ID	Name	Formula	Copies
COA	Coenzyme a	C21 H36 N7 O16 P3 S	1

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:

1BOB 2.3 Å, Histone acetyltransferase HAT1 from saccharomyces cerevisiae in complex with acetyl…
4PSX 2.51 Å, Crystal structure of histone acetyltransferase complex
7XAY 3.3 Å, Crystal structure of Hat1-Hat2-Asf1-H3-H4

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