2DOQ: Sfi1p/Cdc31p complex

crystal structure of Sfi1p/Cdc31p complex. Determined by X-ray diffraction at 3.0 Å resolution. Released 27 Jun 2006.

Method: X-ray diffraction
Resolution: 3.0 Å
Organism: Saccharomyces cerevisiae
Chains: 4
Atoms: 4,230
Mol. weight: 68.84 kDa
Ligands: CA
Released: 27 Jun 2006

Explore 2DOQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2DOQ contains 29 α-helices and 10 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: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	19-31	13
β-strand	39-40	2	1
α-helix	42-51	10
α-helix	58-67	10
β-strand	76-77	2	1
α-helix	78-90	13
α-helix	94-105	12
β-strand	113	1	2
α-helix	115-124	10
α-helix	131-141	11
β-strand	149	1	2
α-helix	151-158	8

Chain B: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	19-32	14
β-strand	39	1	3
α-helix	42-51	10
α-helix	58-67	10
β-strand	77	1	3
α-helix	78-90	13
α-helix	94-105	12
β-strand	112-113	2	4
α-helix	115-124	10
α-helix	131-141	11
β-strand	149-150	2	4
α-helix	151-158	8

Chain C: 10 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	16-18	3
α-helix	19-31	13
β-strand	39-40	2	5
α-helix	42-50	9
α-helix	58-68	11
β-strand	76-77	2	5
α-helix	78-90	13
α-helix	94-105	12
α-helix	115-117	3
α-helix	119-123	5
α-helix	139-141	3
α-helix	151-155	5

Chain D: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	222-238	17
α-helix	239-245	7
α-helix	247-294	48

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cell division control protein 31	A, B, C	protein	161	Saccharomyces cerevisiae	P06704 (AlphaFold model)
SFI1p	D	protein	94	Saccharomyces cerevisiae	Q12369 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>2DOQ_1 Cell division control protein 31 (chains A, B, C)
MSKNRSSLQSGPLNSELLEEQKQEIYEAFSLFDMNNDGFLDYHELKVAMKALGFELPKRE
ILDLIDEYDSEGRHLMKYDDFYIVMGEKILKRDPLDEIKRAFQLFDDDHTGKISIKNLRR
VAKELGETLTDEELRAMIEEFDLDGDGEINENEFIAICTDS

Sequence of entity 2 (D), FASTA

>2DOQ_2 SFI1p (chains D)
GPLGSNEEANRFANQAKLRVQEAVFYIWSDKTLKYSQMANDEAESFRNTWLLFRSFQQWI
TLTQTFKEQSRLADQAFLNKMFRKILKAQEHWKH

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	7

Primary citation

Structural role of Sfi1p-centrin filaments in budding yeast spindle pole body duplication. Li, S., Sandercock, A.M., Conduit, P. et al. J Cell Biol (2006) 173:867-877. DOI 10.1083/jcb.200603153 · 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
3FWC 2.7 Å, Sac3:Sus1:Cdc31 complex
2GV5 3.0 Å, crystal structure of Sfi1p/Cdc31p complex

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