3NWS: Cell division control protein 13

Crystal structure of the N-terminal domain of the yeast telomere-binding and telomerase regulatory protein Cdc13. Determined by X-ray diffraction at 2.5 Å resolution. Released 22 Sept 2010.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Saccharomyces cerevisiae
Chains: 4
Atoms: 6,406
Mol. weight: 100.64 kDa
Released: 22 Sept 2010

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

Secondary structure: helices and β-sheets

3NWS contains 35 α-helices and 28 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: 7 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	16-17	2	1
α-helix	21-24	4
β-strand	31-46	16	1
β-strand	51-56	6	1
β-strand	70-73	4	1
α-helix	79-95	17
β-strand	113-115	3	1
α-helix	118-120	3
β-strand	125-135	11	1
β-strand	138-148	11	1
α-helix	151-157	7
α-helix	178-194	17
α-helix	211-216	6
α-helix	217-221	5

Chain B: 10 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	16-17	2	2
α-helix	21-26	6
β-strand	32-46	15	2
β-strand	51-56	6	2
β-strand	70-73	4	2
α-helix	79-95	17
β-strand	113-115	3	2
α-helix	118-121	4
β-strand	125-135	11	2
β-strand	138-148	11	2
α-helix	149-150	2
α-helix	151-157	7
α-helix	178-194	17
α-helix	203-205	3
α-helix	211-216	6
α-helix	217-222	6
α-helix	223	1

Chain C: 9 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	15	1
β-strand	16-17	2	3
α-helix	21-26	6
β-strand	31-46	16	3
β-strand	51-56	6	3
β-strand	70-73	4	3
α-helix	79-95	17
β-strand	113-115	3	3
α-helix	118-120	3
β-strand	125-135	11	3
β-strand	138-148	11	3
α-helix	151-158	8
α-helix	178-195	18
α-helix	203-205	3
α-helix	211-216	6
α-helix	217-222	6

Chain D: 9 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	16-17	2	4
α-helix	21-26	6
β-strand	31-46	16	4
β-strand	51-56	6	4
β-strand	70-73	4	4
α-helix	79-95	17
β-strand	113-115	3	4
α-helix	118-120	3
β-strand	125-135	11	4
β-strand	138-148	11	4
α-helix	151-157	7
α-helix	178-195	18
α-helix	203-205	3
α-helix	211-216	6
α-helix	217-221	5
α-helix	222-223	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cell division control protein 13	A, B, C, D	protein	219	Saccharomyces cerevisiae	P32797 (AlphaFold model)

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

>3NWS_1 Cell division control protein 13 (chains A, B, C, D)
GHMMKNRIFVSSSKDFEGYPSKAIVPVQFVALLTSIHLTETKCLLGFSNFERRGDQSQED
QYLIKLKFKDRGSERLARITISLLCQYFDIELPDLDSDSGASPTVILRDIHLERLCFSSC
KALYVSKHGNYTLFLEDIKPLDLVSVISTISTKSTNSSKHSSSELISECDLNNSLVDIFN
NLIEMNRDEKNRFKFVKLIHYDIELKKFVQDQQKVLSQK

Primary citation

Cdc13 N-terminal dimerization, DNA binding, and telomere length regulation. Mitchell, M.T., Smith, J.S., Mason, M. et al. Mol Cell Biol (2010) 30:5325-5334. DOI 10.1128/MCB.00515-10 · PubMed

Other PDB entries of the same protein (UniProt P32797 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4HCE 2.3 Å, Crystal structure of the telomeric Saccharomyces cerevisiae Cdc13 OB2 domain
3OIQ 2.4 Å, Crystal structure of yeast telomere protein Cdc13 OB1 and the catalytic subunit of DNA…
3OIP 2.5 Å, Crystal structure of Yeast telomere protein Cdc13 OB1
3NWT 2.7 Å, Crystal structure of the N-terminal domain of the yeast telomere-binding and telomerase…
1KXL Solution Structure of the Cdc13 DNA-binding Domain in a Complex with Single-Stranded…
1S40 Solution structure of the CDC13 DNA-binding domain complexed with a single-stranded…

Browse structure collections

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