2QUQ: Essential Inner Kinetochore Protein Cep3p

Crystal Structure of the Essential Inner Kinetochore Protein Cep3p. Determined by X-ray diffraction at 2.8 Å resolution. Released 13 Nov 2007.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Saccharomyces cerevisiae
Chains: 1
Atoms: 4,307
Mol. weight: 66.09 kDa
Released: 13 Nov 2007

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

Secondary structure: helices and β-sheets

2QUQ contains 34 α-helices and 4 β-strands across 1 chain. 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: 34 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	58-68	11
α-helix	69-76	8
α-helix	77-78	2
α-helix	94-105	12
α-helix	108-120	13
α-helix	123-130	8
α-helix	134-145	12
α-helix	146-148	3
α-helix	154-173	20
α-helix	176-180	5
α-helix	186-192	7
α-helix	200-204	5
α-helix	211-220	10
α-helix	231-241	11
α-helix	245-248	4
α-helix	250-265	16
α-helix	280-302	23
β-strand	305	1	1
β-strand	308	1	1
α-helix	313-315	3
α-helix	342-356	15
α-helix	367-385	19
α-helix	394-417	24
α-helix	418-422	5
α-helix	427-443	17
α-helix	446-448	3
α-helix	451-455	5
α-helix	457-476	20
α-helix	480-493	14
α-helix	498-500	3
α-helix	501-522	22
α-helix	525-526	2
β-strand	527-528	2	2
β-strand	533-534	2	2
α-helix	536-550	15
α-helix	555-561	7
α-helix	590-600	11
α-helix	603-605	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Centromere DNA-binding protein complex CBF3 subunit B	A	protein	562	Saccharomyces cerevisiae	P40969 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2QUQ_1 Centromere DNA-binding protein complex CBF3 subunit B (chains A)
KLITASSSKEYLPDLLLFWQNYEYWITNIGLYKTKQRDLTRTPANLDTDTEECMFWMNYL
QKDQSFQLMNFAMENLGALYFGSIGDISELYLRVEQYWDRRADKNHSVDGKYWDALIWSV
FTMCIYYMPVEKLAEIFSVYPLHEYLGSNKRLNWEDGMQLVMCQNFARCSLFQLKQCDFM
AHPDIRLVQAYLILATTTFPYDEPLLANSLLTQCIHTFKNFHVDDFRPLLNDDPVESIAK
VTLGRIFYRLCGCDYLQSGPRKPIALHTEVSSLLQHAAYLQDLPNVDVYREENSTEVLYW
KIISLDRDLDQYLNKSSKPPLKTLDAIRRELDIFQYKVDSLEEDFRSNNSRFQKFIALFQ
ISTVSWKLFKMYLIYYDTADSLLKVIHYSKVIISLIVNNFHAKSEFFNRHPMVMQTITRV
VSFISFYQIFVESAAVKQLLVDLTELTANLPTIFGSKLDKLVYLTERLSKLKLLWDKVQL
LDSGDSFYHPVFKILQNDIKIIELKNDEMFSLIKGLGSLVPLNKLRQESLLEEEDENNTE
PSDFRTIVEEFQSEYNISDILS

Primary citation

Crystal structure of the yeast inner kinetochore subunit Cep3p. Bellizzi, J.J., Sorger, P.K., Harrison, S.C. Structure (2007) 15:1422-1430. DOI 10.1016/j.str.2007.09.008 · PubMed

Other PDB entries of the same protein (UniProt P40969 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2VEQ 2.49 Å, Insights into kinetochore-DNA interactions from the structure of Cep3p
6GYU 3.0 Å, Cryo-EM structure of the CBF3-msk complex of the budding yeast kinetochore
10EH 3.5 Å, De novo assembled CBF3-CEN complex
6F07 3.6 Å, CBF3 Core Complex
6GYP 3.6 Å, Cryo-EM structure of the CBF3-core-Ndc10-DBD complex of the budding yeast kinetochore
6FE8 3.7 Å, Cryo-EM structure of the core Centromere Binding Factor 3 complex
8OW1 3.7 Å, Cryo-EM structure of the yeast Inner kinetochore bound to a CENP-A nucleosome.
7K79 4.0 Å, CBF3
6GSA 4.2 Å, Core Centromere Binding Factor 3 (CBF3) with monomeric Ndc10
7K7G 4.2 Å, nucleosome and Gal4 complex
6GYS 4.4 Å, Cryo-EM structure of the CBF3-CEN3 complex of the budding yeast kinetochore

Browse structure collections

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