3OAK: Spn1 (Iws1)-Spt6 complex

Crystal structure of a Spn1 (Iws1)-Spt6 complex. Determined by X-ray diffraction at 2.15 Å resolution. Released 24 Nov 2010.

Method: X-ray diffraction
Resolution: 2.15 Å
Organism: Saccharomyces cerevisiae
Chains: 4
Atoms: 3,171
Mol. weight: 41.54 kDa
Released: 24 Nov 2010

Explore 3OAK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3OAK contains 27 α-helices and 0 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: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	149-181	33
α-helix	191-203	13
α-helix	206-208	3
α-helix	209-214	6
α-helix	217-225	9
α-helix	227-228	2
α-helix	232-235	4
α-helix	236-248	13
α-helix	253-259	7
α-helix	261-270	10
α-helix	276-289	14

Chain B: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	150-182	33
α-helix	191-203	13
α-helix	206-208	3
α-helix	209-214	6
α-helix	218-225	8
α-helix	227-228	2
α-helix	232-235	4
α-helix	236-248	13
α-helix	253-259	7
α-helix	261-268	8
α-helix	276-290	15

Chain C: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	234-249	16
α-helix	256-262	7

Chain D: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	238-240	3
α-helix	241-249	9
α-helix	256-262	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transcription factor IWS1	A, B	protein	151	Saccharomyces cerevisiae	Q06505 (AlphaFold model)
Transcription elongation factor SPT6	C, D	protein	31	Saccharomyces cerevisiae	P23615 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3OAK_1 Transcription factor IWS1 (chains A, B)
GIDPFTDDLEQYLDEKILRLKDEMNIAAQLDIDTLNKRIETGDTSLIAMQKVKLLPKVVS
VLSKANLADTILDNNLLQSVRIWLEPLPDGSLPSFEIQKSLFAALNDLPVKTEHLKESGL
GRVVIFYTKSKRVEAQLARLAEKLIAEWTRP

Sequence of entity 2 (C, D), FASTA

>3OAK_2 Transcription elongation factor SPT6 (chains C, D)
DPFTHMSDKIDEMYDIFGDGHDYDWALEIEN

Primary citation

Structure and biological importance of the spn1-spt6 interaction, and its regulatory role in nucleosome binding. McDonald, S.M., Close, D., Xin, H. et al. Mol Cell (2010) 40:725-735. DOI 10.1016/j.molcel.2010.11.014 · PubMed

Other PDB entries of the same protein (UniProt Q06505 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3NFQ 1.85 Å, Crystal structure of the conserved central domain of yeast Spn1/Iws1
3O8Z 2.15 Å, Crystal structure of Spn1 (Iws1) core domain

Browse structure collections

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