4WNN: SPT16-H2A-H2B FACT HISTONE Complex

SPT16-H2A-H2B FACT HISTONE Complex. Determined by X-ray diffraction at 1.8 Å resolution. Released 21 Oct 2015.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Saccharomyces cerevisiae
Chains: 9
Atoms: 6,166
Mol. weight: 104.01 kDa
Ligands: PO4
Released: 21 Oct 2015

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

Secondary structure: helices and β-sheets

4WNN contains 40 α-helices and 18 β-strands across 9 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: 5 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	18-22	5
α-helix	28-37	10
β-strand	43-44	2	1
α-helix	47-73	27
β-strand	78-79	2	2
α-helix	81-89	9
α-helix	92-98	7

Chain B: 5 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	35-38	4
α-helix	41-51	11
β-strand	56-57	2	2
α-helix	59-86	28
β-strand	91-92	2	1
α-helix	94-104	11
α-helix	107-125	19

Chain C: 5 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	18-22	5
α-helix	28-37	10
β-strand	43-44	2	3
α-helix	47-73	27
β-strand	78-79	2	4
α-helix	81-89	9
α-helix	92-97	6

Chain D: 6 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	31	1
α-helix	33-35	3
α-helix	41-51	11
β-strand	56-57	2	4
β-strand	58	1	5
α-helix	59-86	28
β-strand	91-92	2	3
α-helix	94-104	11
α-helix	107-125	19

Chain E: 5 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	18-21	4
α-helix	28-37	10
β-strand	43-44	2	6
α-helix	47-73	27
β-strand	78-79	2	7
α-helix	81-90	10
α-helix	92-98	7

Chain F: 5 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	35-38	4
α-helix	41-51	11
β-strand	56-57	2	7
α-helix	59-86	28
β-strand	91-92	2	6
α-helix	94-104	11
α-helix	107-124	18

Chain G: 5 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	18-22	5
α-helix	28-36	9
β-strand	43-44	2	8
α-helix	47-71	25
β-strand	78-79	2	9
α-helix	81-89	9
α-helix	92-97	6

Chain H: 4 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	41-51	11
β-strand	56-57	2	9
α-helix	59-86	28
β-strand	91-92	2	8
α-helix	94-104	11
α-helix	107-124	18

1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone H2A.1	A, C, E, G	protein	132	Saccharomyces cerevisiae	P04911 (AlphaFold model)
Histone H2B.1	B, D, F, H	protein	102	Saccharomyces cerevisiae	P02293 (AlphaFold model)
SPT16	T	protein	20	Saccharomyces cerevisiae	P32558 (AlphaFold model)

Sequence of entity 1 (A, C, E, G), FASTA

>4WNN_1 Histone H2A.1 (chains A, C, E, G)
MSGGKGGKAGSAAKASQSRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYL
AAEILELAGNAARDNKKTRIIPRHLQLAIRNDDELNKLLGNVTIAQGGVLPNIHQNLLPK
KSAKATKASQEL

Sequence of entity 2 (B, D, F, H), FASTA

>4WNN_2 Histone H2B.1 (chains B, D, F, H)
MKKRSKARKETYSSYIYKVLKQTHPDTGISQKSMSILNSFVNDIFERIATEASKLAAYNK
KSTISAREIQTAVRLILPGELAKHAVSEGTRAVTKYSSSTQA

Sequence of entity 3 (T), FASTA

>4WNN_3 SPT16 (chains T)
GIKKTDDEASDESEEEVSEY

Ligands and cofactors

ID	Name	Formula	Copies
PO4	Phosphate ion	O4 P	2

Primary citation

FACT Disrupts Nucleosome Structure by Binding H2A-H2B with Conserved Peptide Motifs. Kemble, D.J., McCullough, L.L., Whitby, F.G. et al. Mol Cell (2015) 60:294-306. DOI 10.1016/j.molcel.2015.09.008 · PubMed

Other PDB entries of the same protein (UniProt P04911 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3T7K 2.03 Å, Complex structure of Rtt107p and phosphorylated histone H2A
7DLX 2.4 Å, crystal structure of H2AM4>Z-H2B
5BT1 2.62 Å, histone chaperone Hif1 playing with histone H2A-H2B dimer
9C9G 2.91 Å, S.c INO80 in complex with S.c 0/80 nucleosome
9C9S 3.09 Å, S.c INO80 in complex with S.c 0/40 nucleosome, Class 1
1ID3 3.1 Å, Crystal structure of the yeast nucleosome core particle reveals fundamental differences…
7K78 3.1 Å, antibody and nucleosome complex
9C9T 3.16 Å, S.c INO80 in complex with S.c 0/40 nucleosome, Class 2
7SSA 3.2 Å, Cryo-EM structure of pioneer factor Cbf1 bound to the nucleosome
9OB1 3.2 Å, S.c INO80 in complex with Yeast 0/80 nucleosome, Apo State
7ON1 3.35 Å, Cenp-A nucleosome in complex with Cenp-C
8OW0 3.4 Å, Cryo-EM structure of CBF1-CCAN bound topologically to a centromeric CENP-A nucleosome

Browse structure collections

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