3FWC: Sac3:Sus1:Cdc31 complex

Sac3:Sus1:Cdc31 complex. Determined by X-ray diffraction at 2.7 Å resolution. Released 14 Apr 2009.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: Saccharomyces cerevisiae
Chains: 16
Atoms: 13,510
Mol. weight: 204.75 kDa
Released: 14 Apr 2009

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

Secondary structure: helices and β-sheets

3FWC contains 76 α-helices and 16 β-strands across 16 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	19-30	12
β-strand	39-40	2	1
α-helix	42-50	9
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	151-158	8

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	726-803	78

Chain C: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	9-18	10
α-helix	21-35	15
α-helix	38-50	13
α-helix	58-70	13
α-helix	75-90	16

Chain D: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	9-18	10
α-helix	21-35	15
α-helix	38-52	15
α-helix	58-72	15
α-helix	75-89	15

Chain E: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	19-31	13
β-strand	39-40	2	3
α-helix	42-50	9
α-helix	58-68	11
β-strand	76-77	2	3
α-helix	78-90	13
α-helix	94-105	12
β-strand	112-113	2	4
α-helix	115-125	11
α-helix	131-140	10
β-strand	149-150	2	4
α-helix	151-159	9

Chain F: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	723-803	81

Chain G: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	7-18	12
α-helix	21-36	16
α-helix	38-51	14
α-helix	59-70	12
α-helix	78-92	15

Chain H: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	5-18	14
α-helix	21-35	15
α-helix	38-52	15
α-helix	58-72	15
α-helix	75-90	16

8 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
Cell division control protein 31	A, E, I, M	protein	161	Saccharomyces cerevisiae	P06704 (AlphaFold model)
Nuclear mRNA export protein SAC3	B, F, J, N	protein	85	Saccharomyces cerevisiae	P46674 (AlphaFold model)
Protein SUS1	C, D, G, H, K, L, O, P	protein	96	Saccharomyces cerevisiae	Q6WNK7 (AlphaFold model)

Sequence of entity 1 (A, E, I, M), FASTA

>3FWC_1 Cell division control protein 31 (chains A, E, I, M)
MSKNRSSLQSGPLNSELLEEQKQEIYEAFSLFDMNNDGFLDYHELKVAMKALGFELPKRE
ILDLIDEYDSEGRHLMKYDDFYIVMGEKILKRDPLDEIKRAFQLFDDDHTGKISIKNLRR
VAKELGETLTDEELRAMIEEFDLDGDGEINENEFIAICTDS

Sequence of entity 2 (B, F, J, N), FASTA

>3FWC_2 Nuclear mRNA export protein SAC3 (chains B, F, J, N)
GSKQVITEQIANDLVKEVVNSSVISIVKREFSEANYRKDFIDTMTRELYDAFLHERLYLI
YMDSRAELKRNSTLKKKFFEKWQAS

Sequence of entity 3 (C, D, G, H, K, L, O, P), FASTA

>3FWC_3 Protein SUS1 (chains C, D, G, H, K, L, O, P)
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:

3FWB 2.5 Å, Sac3:Sus1:Cdc31 complex
4MBE 2.61 Å, Sac3:Sus1:Cdc31:Nup1 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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