3FWB: Sac3:Sus1:Cdc31 complex

Sac3:Sus1:Cdc31 complex. Determined by X-ray diffraction at 2.5 Å resolution. Released 14 Apr 2009.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Saccharomyces cerevisiae
Chains: 3
Atoms: 2,506
Mol. weight: 36.64 kDa
Released: 14 Apr 2009

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

Secondary structure: helices and β-sheets

3FWB contains 14 α-helices and 4 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: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	19-32	14
β-strand	39-40	2	1
α-helix	42-51	10
α-helix	58-68	11
β-strand	76-77	2	1
α-helix	78-90	13
α-helix	94-105	12
β-strand	112-113	2	2
α-helix	115-124	10
α-helix	131-139	9
β-strand	149-150	2	2
α-helix	151-160	10

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	753-803	51

Chain C: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	8-18	11
α-helix	21-35	15
α-helix	38-51	14
α-helix	58-71	14
α-helix	75-90	16

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cell division control protein 31	A	protein	161	Saccharomyces cerevisiae	P06704 (AlphaFold model)
Nuclear mRNA export protein SAC3	B	protein	55	Saccharomyces cerevisiae	P46674 (AlphaFold model)
Protein SUS1	C	protein	96	Saccharomyces cerevisiae	Q6WNK7 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3FWB_1 Cell division control protein 31 (chains A)
MSKNRSSLQSGPLNSELLEEQKQEIYEAFSLFDMNNDGFLDYHELKVAMKALGFELPKRE
ILDLIDEYDSEGRHLMKYDDFYIVMGEKILKRDPLDEIKRAFQLFDDDHTGKISIKNLRR
VAKELGETLTDEELRAMIEEFDLDGDGEINENEFIAICTDS

Sequence of entity 2 (B), FASTA

>3FWB_2 Nuclear mRNA export protein SAC3 (chains B)
GSEANYRKDFIDTMTRELYDAFLHERLYLIYMDSRAELKRNSTLKKKFFEKWQAS

Sequence of entity 3 (C), FASTA

>3FWB_3 Protein SUS1 (chains C)
MTMDTAQLKSQIQQYLVESGNYELISNELKARLLQEGWVDKVKDLTKSEMNINESTNFTQ
ILSTVEPKALEMVSDSTRETVLKQIREFLEEIVDTQ

Primary citation

Sus1, Cdc31, and the Sac3 CID region form a conserved interaction platform that promotes nuclear pore association and mRNA export. Jani, D., Lutz, S., Marshall, N.J. et al. Mol Cell (2009) 33:727-737. DOI 10.1016/j.molcel.2009.01.033 · PubMed

Other PDB entries of the same protein (UniProt P06704 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4MBE 2.61 Å, Sac3:Sus1:Cdc31:Nup1 complex
3FWC 2.7 Å, Sac3:Sus1:Cdc31 complex
2DOQ 3.0 Å, crystal structure of Sfi1p/Cdc31p complex
2GV5 3.0 Å, crystal structure of Sfi1p/Cdc31p complex

Browse structure collections

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