6CW2: Histone acetyltransferase GCN5

Crystal structure of a yeast SAGA transcriptional coactivator Ada2/Gcn5 HAT subcomplex, crystal form 1. Determined by X-ray diffraction at 2.67 Å resolution. Released 19 Sept 2018.

Method: X-ray diffraction
Resolution: 2.67 Å
Organisms: Saccharomyces cerevisiae, Homo sapiens
Chains: 4
Atoms: 5,948
Mol. weight: 90.97 kDa
Ligands: ZN
Released: 19 Sept 2018

Explore 6CW2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6CW2 contains 32 α-helices and 57 β-strands across 4 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: 10 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	6-10	5	5
β-strand	13-15	3	6
β-strand	21-28	8	5
α-helix	32-34	3
β-strand	37-42	6	6
β-strand	48-55	8	6
α-helix	56-58	3
β-strand	60-63	4	6
β-strand	71-76	6	5
α-helix	77-79	3
β-strand	81-86	6	5
α-helix	91-93	3
β-strand	95-102	8	6
α-helix	103	1
β-strand	113	1	3
β-strand	119-122	4	6
β-strand	126-130	5	6
α-helix	133-135	3
β-strand	136	1	7
α-helix	137-138	2
β-strand	139-143	5	8
β-strand	157-164	8	8
β-strand	165	1	7
β-strand	170-173	4	9
α-helix	174-176	3
β-strand	182-184	3	8
α-helix	185-187	3
β-strand	188-189	2	8
β-strand	195-201	7	8
β-strand	213-219	7	9
α-helix	220-222	3
β-strand	224-230	7	9

Chain B: 6 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	5-8	4	10
β-strand	11-15	5	11
β-strand	20-26	7	10
β-strand	34-39	6	11
α-helix	44-45	2
β-strand	46-50	5	11
β-strand	54-55	2	11
β-strand	63-68	6	10
β-strand	71-76	6	10
α-helix	81-83	3
β-strand	85-91	7	11
β-strand	99	1	11
β-strand	103-108	6	11
β-strand	112	1	12
α-helix	113-114	2
β-strand	115-119	5	13
α-helix	120-122	3
α-helix	123-127	5
β-strand	131-140	10	13
β-strand	141	1	12
β-strand	146-147	2	14
β-strand	160-164	5	13
α-helix	165-168	4
β-strand	174-182	9	13
β-strand	194-198	5	14
β-strand	206-209	4	14

Chain C: 5 helices, 4 β-strands

Element	Residues	Length	Sheet
β-strand	7	1	4
β-strand	19-22	4	4
β-strand	29-30	2	4
α-helix	32-36	5
β-strand	50-53	4	4
α-helix	67-80	14
α-helix	85-92	8
α-helix	97-104	8
α-helix	105-109	5

Chain D: 11 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	74-79	6	1
β-strand	82-87	6	1
α-helix	90-96	7
β-strand	100-105	6	2
α-helix	111-127	17
α-helix	133-141	9
β-strand	146-152	7	2
β-strand	156-166	11	2
α-helix	167-169	3
β-strand	171-179	9	2
α-helix	188-203	16
β-strand	208-213	6	2
α-helix	215-223	9
β-strand	226-227	2	2
α-helix	234-237	4
β-strand	248-253	6	2
β-strand	258	1	3
α-helix	260-262	3
α-helix	263-279	17
α-helix	286-287	2
β-strand	288	1	4
α-helix	289-291	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone acetyltransferase GCN5	D	protein	251	Saccharomyces cerevisiae	Q03330 (AlphaFold model)
Transcriptional adapter 2	C	protein	120	Saccharomyces cerevisiae	Q02336 (AlphaFold model)
antibody heavy chain	A	protein	229	Homo sapiens
antibody light chain	B	protein	215	Homo sapiens

Sequence of entity 1 (D), FASTA

>6CW2_1 Histone acetyltransferase GCN5 (chains D)
VTDVEKGIVKFEFDGVEYTFKERPSVVEENEGKIEFRVVNNDNTKENMMVLTGLKNIFQK
QLPKMPKEYIARLVYDRSHLSMAVIRKPLTVVGGITYRPFDKREFAEIVFCAISSTEQVR
GYGAHLMNHLKDYVRNTSNIKYFLTYADNYAIGYFKKQGFTKEITLDKSIWMGYIKDYEG
GTLMQCSMLPRIRYLDAGKILLLQEAALRRKIRTISKSHIVRPGLEQFKDLNNIKPIDPM
TIPGLKEAGWT

Sequence of entity 2 (C), FASTA

>6CW2_2 Transcriptional adapter 2 (chains C)
MSNKFHCDVCSADCTNRVRVSCAICPEYDLCVPCFSQGSYTGKHRPYHDYRIIETNSYPI
LCPDWGADEELQLIKGAQTLGLGNWQDIADHIGSRGKEEVKEHYLKYYLESKYYPIPDIT

Sequence of entity 3 (A), FASTA

>6CW2_3 antibody heavy chain (chains A)
EVQLVESGGGLVQPGGSLRLSCAASGFNVSYSSIHWVRQAPGKGLEWVASIYPYYGSTSY
ADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARNWYWFGGHFGYYMMPWAMDYWG
QGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVH
TFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEP

Sequence of entity 4 (B), FASTA

>6CW2_4 antibody light chain (chains B)
SDIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVP
SRFSGSRSGTDFTLTISSLQPEDFATYYCQQSSWYPVTFGQGTKVEIKRTVAAPSVFIFP
PSDSQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL
TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	2

Primary citation

Structural basis for activation of SAGA histone acetyltransferase Gcn5 by partner subunit Ada2. Sun, J., Paduch, M., Kim, S.A. et al. Proc Natl Acad Sci U S A (2018) 115:10010-10015. DOI 10.1073/pnas.1805343115 · PubMed

Other PDB entries of the same protein (UniProt Q03330 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1E6I 1.87 Å, Bromodomain from GCN5 complexed with acetylated H4 peptide
1YGH 1.9 Å, Hat domain of GCN5 from saccharomyces cerevisiae
6CW3 1.98 Å, Crystal structure of a yeast SAGA transcriptional coactivator Ada2/Gcn5 HAT subcomplex,…

Browse structure collections

About this viewer

MolViewer shows 6CW2 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.