1TVK: Tubulin alpha chain

The binding mode of epothilone A on a,b-tubulin by electron crystallography. Determined by electron crystallography at 2.89 Å resolution. Released 14 Sept 2004.

Method: Electron crystallography
Resolution: 2.89 Å
Organism: Bos taurus
Chains: 2
Atoms: 6,672
Mol. weight: 98.27 kDa
Ligands: GTP, GDP, EP
Released: 14 Sept 2004

Explore 1TVK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1TVK contains 39 α-helices and 44 β-strands across 2 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: 18 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	1
α-helix	10-26	17
β-strand	67-68	2	1
α-helix	72-76	5
α-helix	84-86	3
α-helix	103-104	2
α-helix	105-109	5
α-helix	112-127	16
β-strand	132-138	7	1
α-helix	145-149	5
α-helix	150-158	9
β-strand	165-168	4	1
β-strand	171-172	2	2
α-helix	184-195	12
β-strand	200-201	2	1
β-strand	203	1	3
β-strand	204-205	2	2
α-helix	206-213	8
α-helix	224-227	4
α-helix	232-238	7
α-helix	252-259	8
β-strand	269	1	3
β-strand	277	1	4
α-helix	288-295	8
β-strand	312-314	3	5
β-strand	315	1	6
β-strand	318-320	3	7
α-helix	328-335	8
β-strand	343	1	5
β-strand	351	1	6
β-strand	354-356	3	7
β-strand	368	1	4
β-strand	380-381	2	5
α-helix	385-399	15
α-helix	406-409	4
α-helix	415-432	18

Chain B: 21 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	8
β-strand	9	1	9
α-helix	10-20	11
α-helix	26-28	3
β-strand	30	1	10
β-strand	36	1	10
α-helix	47-49	3
β-strand	53	1	11
β-strand	59	1	11
β-strand	63	1	8
β-strand	65	1	12
β-strand	66	1	9
α-helix	73-77	5
β-strand	90	1	12
α-helix	101-102	2
α-helix	103-107	5
α-helix	116-124	9
β-strand	130-134	5	8
β-strand	136-138	3	13
α-helix	146-155	10
β-strand	163-164	2	8
β-strand	167-170	4	13
α-helix	171-172	2
α-helix	181-192	12
β-strand	199-200	2	14
β-strand	202-203	2	13
α-helix	206-212	7
α-helix	222-236	15
α-helix	238-240	3
β-strand	244	1	15
α-helix	250-257	8
β-strand	265-266	2	14
β-strand	268-269	2	16
α-helix	289-293	5
β-strand	299	1	16
α-helix	305-307	3
β-strand	310	1	17
β-strand	316-318	3	15
α-helix	323-335	13
α-helix	338-340	3
β-strand	352-354	3	15
β-strand	364-366	3	15
β-strand	367-368	2	16
β-strand	371	1	17
α-helix	377-389	13
α-helix	395-399	5
α-helix	407-423	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tubulin alpha chain	A	protein	440	Bos taurus	Q2HJ86 (AlphaFold model)
Tubulin beta chain	B	protein	427	Bos taurus	Q6B856 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1TVK_1 Tubulin alpha chain (chains A)
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK
HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFSVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA
VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRGHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYEPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE
AREDMAALEKDYEEVGVDSV

Sequence of entity 2 (B), FASTA

>1TVK_2 Tubulin beta chain (chains B)
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYV
PRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVV
EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMM
AACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG
LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQD

Ligands and cofactors

ID	Name	Formula	Copies
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	1
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	1
EP	Epothilone a	C26 H39 N O6 S	1

Primary citation

The binding mode of epothilone A on alpha,beta-tubulin by electron crystallography. Nettles, J.H., Li, H., Cornett, B. et al. Science (2004) 305:866-869. DOI 10.1126/science.1099190 · PubMed

Other PDB entries of the same protein (UniProt Q2HJ86 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7RRO 3.4 Å, Structure of the 48-nm repeat doublet microtubule from bovine tracheal cilia
9CPB 3.52 Å, Atomic model of bovine Fallopian tube cilia doublet microtubule (48-nm periodicity)
1SA0 3.58 Å, Tubulin-colchicine: stathmin-like domain complex
1Z2B 4.1 Å, Tubulin-colchicine-vinblastine: stathmin-like domain complex
1SA1 4.2 Å, Tubulin-podophyllotoxin: stathmin-like domain complex
2XRP 8.2 Å, Human Doublecortin N-DC Repeat (1MJD) and Mammalian Tubulin (1JFF and 3HKE) Docked into…
4ATX 8.2 Å, Rigor kinesin motor domain with an ordered neck-linker, docked on tubulin dimer,…
4ATU 8.3 Å, Human doublecortin N-DC repeat plus linker, and tubulin (2XRP) docked into an 8A cryo-EM…
3IZ0 8.6 Å, Human Ndc80 Bonsai Decorated Microtubule
4CK6 9.2 Å, Pseudo-atomic model of microtubule-bound human kinesin-5 motor domain in the ADP.AlFx…
4CK7 9.2 Å, Pseudo-atomic model of microtubule-bound human kinesin-5 motor domain in presence of…
5M5I 9.3 Å, Pseudo-atomic model of microtubule-bound S.pombe kinesin-5 motor domain in the AMPPNP…

Browse structure collections

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