4ICU: Tubulin-specific chaperone E

Name: PDB 4ICU: Ubiquitin-like domain of human tubulin folding cofactor E - crystal from A
Published: 2014-06-18
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: chaperone

Ubiquitin-like domain of human tubulin folding cofactor E - crystal from A. Determined by X-ray diffraction at 2.4 Å resolution. Released 18 Jun 2014.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: Homo sapiens
Chains: 4
Atoms: 2,838
Mol. weight: 39.28 kDa
Released: 18 Jun 2014

Explore 4ICU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4ICU contains 11 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: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	445-451	7	1
β-strand	461-466	6	1
β-strand	470	1	2
α-helix	471-482	12
α-helix	486-488	3
β-strand	490-494	5	1
α-helix	502	1
β-strand	503-504	2	1
β-strand	511	1	2
α-helix	513-515	3
β-strand	522-526	5	1

Chain B: 2 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	445-451	7	3
β-strand	459-466	8	3
β-strand	470	1	4
α-helix	471-482	12
α-helix	486-488	3
β-strand	490-495	6	3
β-strand	498-504	7	3
β-strand	511	1	4
β-strand	522-526	5	3

Chain C: 3 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	445-451	7	5
β-strand	461-466	6	5
β-strand	470	1	6
α-helix	471-482	12
α-helix	486-488	3
β-strand	490-494	5	5
α-helix	502	1
β-strand	503-504	2	5
β-strand	511	1	6
β-strand	522-526	5	5

Chain D: 2 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	445-451	7	7
β-strand	461-466	6	7
β-strand	470	1	8
α-helix	471-482	12
α-helix	486-488	3
β-strand	490-494	5	7
β-strand	503-504	2	7
β-strand	511	1	8
β-strand	522-526	5	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tubulin-specific chaperone E	A, B, C, D	protein	85	Homo sapiens	Q15813 (AlphaFold model)

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

>4ICU_1 Tubulin-specific chaperone E (chains A, B, C, D)
NQLLTLKIKYPHQLDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYESPKKPGRE
IELENDLKSLQFYSVENGDCLLVRW

Primary citation

The structure of the complex between alpha-tubulin, TBCE and TBCB reveals a tubulin dimer dissociation mechanism. Serna, M., Carranza, G., Martin-Benito, J. et al. J Cell Sci (2015) 128:1824-1834. DOI 10.1242/jcs.167387 · PubMed

Other PDB entries of the same protein (UniProt Q15813 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4ICV 1.45 Å, Ubiquitin-like domain of human tubulin folding cofactor E - crystal form B
9M1J 2.14 Å, Cryo-EM structure of the TBC-DE-Arl2-beta-tubulin complex
9M1M 2.21 Å, Cryo-EM structure of the TBC-DEC-Arl2-alpha-beta-tubulin complex with GDP-AlFx
9M1K 2.45 Å, Cryo-EM structure of the TBC-DE-Arl2-beta-tubulin complex with GTP
9M1L 2.55 Å, Cryo-EM structure of the TBC-DE-Arl2-alpha-beta-tubulin complex with GTP

Browse structure collections

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