2VEQ: PDB entry 2VEQ

Insights into kinetochore-DNA interactions from the structure of Cep3p. Determined by X-ray diffraction at 2.49 Å resolution. Released 25 Dec 2007.

Method: X-ray diffraction
Resolution: 2.49 Å
Organism: SACCHAROMYCES CEREVISIAE
Chains: 1
Atoms: 4,405
Mol. weight: 66.59 kDa
Ligands: CAC
Released: 25 Dec 2007

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

Secondary structure: helices and β-sheets

2VEQ contains 33 α-helices and 3 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: 33 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	50-51	2	1
α-helix	58-68	11
α-helix	69-76	8
α-helix	77-79	3
α-helix	85-87	3
α-helix	96-105	10
α-helix	108-121	14
α-helix	123-130	8
α-helix	134-146	13
α-helix	154-173	20
α-helix	176-182	7
α-helix	186-192	7
α-helix	200-202	3
α-helix	204-222	19
α-helix	231-240	10
α-helix	245-248	4
α-helix	250-265	16
α-helix	280-302	23
α-helix	338-356	19
α-helix	364-366	3
α-helix	367-385	19
α-helix	394-417	24
α-helix	418-422	5
α-helix	427-443	17
α-helix	444-446	3
α-helix	451-455	5
α-helix	457-476	20
α-helix	480-495	16
α-helix	498-500	3
α-helix	501-522	22
β-strand	527-528	2	1
β-strand	533-534	2	1
α-helix	536-550	15
α-helix	555-562	8
α-helix	589-600	12
α-helix	603-606	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Centromere DNA-binding protein complex CBF3 subunit B	A	protein	565	SACCHAROMYCES CEREVISIAE	P40969 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2VEQ_1 CENTROMERE DNA-BINDING PROTEIN COMPLEX CBF3 SUBUNIT B (chains A)
GSHMLITASSSKEYLPDLLLFWQNYEYWITNIGLYKTKQRDLTRTPANLDTDTEECMFWM
NYLQKDQSFQLMNFAMENLGALYFGSIGDISELYLRVEQYWDRRADKNHSVDGKYWDALI
WSVFTMCIYYMPVEKLAEIFSVYPLHEYLGSNKRLNWEDGMQLVMCQNFARCSLFQLKQC
DFMAHPDIRLVQAYLILATTTFPYDEPLLANSLLTQCIHTFKNFHVDDFRPLLNDDPVES
IAKVTLGRIFYRLCGCDYLQSGPRKPIALHTEVSSLLQHAAYLQDLPNVDVYREENSTEV
LYWKIISLDRDLDQYLNKSSKPPLKTLDAIRRELDIFQYKVDSLEEDFRSNNSRFQKFIA
LFQISTVSWKLFKMYLIYYDTADSLLKVIHYSKVIISLIVNNFHAKSEFFNRHPMVMQTI
TRVVSFISFYQIFVESAAVKQLLVDLTELTANLPTIFGSKLDKLVYLTERLSKLKLLWDK
VQLLDSGDSFYHPVFKILQNDIKIIELKNDEMFSLIKGLGSLVPLNKLRQESLLEEEDEN
NTEPSDFRTIVEEFQSEYNISDILS

Ligands and cofactors

ID	Name	Formula	Copies
CAC	Cacodylate ion	C2 H6 As O2	1

Water and common crystallization additives (BME) are not listed.

Primary citation

Insights Into Kinetochore-DNA Interactions from the Structure of Cep3Delta. Purvis, A., Singleton, M.R. EMBO Rep (2008) 9:56. DOI 10.1038/SJ.EMBOR.7401139 · PubMed

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

2QUQ 2.8 Å, Crystal Structure of the Essential Inner Kinetochore Protein 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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