9WDA: Tubulin alpha-1A chain

Paclitaxel/GMPCPP-stabilized human alpha1A/beta3 microtubule. Determined by electron microscopy at 2.35 Å resolution. Released 1 Apr 2026.

Method: Electron microscopy
Resolution: 2.35 Å
Organism: Homo sapiens
Chains: 2
Atoms: 6,851
Mol. weight: 102.62 kDa
Ligands: MG, GTP, TA1, G2P
Released: 1 Apr 2026

Explore 9WDA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9WDA contains 54 α-helices and 34 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: 26 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	1
α-helix	10-28	19
β-strand	35	1	2
α-helix	49-51	3
β-strand	53-55	3	3
β-strand	60	1	2
β-strand	61-63	3	3
β-strand	65-69	5	1
α-helix	73-79	7
α-helix	89-91	3
β-strand	92-94	3	1
α-helix	103-104	2
α-helix	105-109	5
α-helix	110-127	18
β-strand	134-140	7	1
α-helix	148-160	13
β-strand	165-172	8	1
α-helix	173-174	2
α-helix	183-189	7
α-helix	191-196	6
β-strand	200-205	6	1
α-helix	206-215	10
α-helix	224-238	15
α-helix	240-242	3
β-strand	248	1	4
α-helix	252-257	6
β-strand	268-273	6	4
α-helix	290-295	6
α-helix	298-300	3
α-helix	307-309	3
β-strand	312-321	10	4
α-helix	325-336	12
β-strand	343	1	4
β-strand	351-356	6	4
α-helix	358-360	3
α-helix	362-363	2
α-helix	368-370	3
β-strand	373-381	9	4
α-helix	382-384	3
α-helix	385-400	16
α-helix	405-409	5
α-helix	416-434	19

Chain b: 28 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	5-9	5	5
α-helix	10-28	19
β-strand	30	1	6
β-strand	35	1	7
β-strand	36	1	6
α-helix	41-44	4
α-helix	47-49	3
β-strand	51-54	4	7
β-strand	58-61	4	7
β-strand	63-67	5	5
α-helix	71-78	8
α-helix	87-89	3
β-strand	90-92	3	5
α-helix	101-102	2
α-helix	103-107	5
α-helix	108-125	18
β-strand	132-138	7	5
α-helix	143-147	5
α-helix	148-158	11
β-strand	163-169	7	5
α-helix	181-187	7
α-helix	189-195	7
β-strand	198-202	5	5
α-helix	204-213	10
α-helix	222-236	15
α-helix	238-240	3
β-strand	246	1	5
α-helix	250-255	6
β-strand	265-271	7	5
α-helix	278-281	4
α-helix	286-294	9
α-helix	296-298	3
β-strand	299	1	5
α-helix	305-307	3
β-strand	310-318	9	5
α-helix	323-336	14
α-helix	338-340	3
β-strand	341	1	5
β-strand	349-354	6	5
α-helix	357-358	2
β-strand	364-371	8	5
α-helix	372-374	3
α-helix	375-390	16
α-helix	396-399	4
α-helix	406-415	10
α-helix	421-424	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tubulin alpha-1A chain	a	protein	451	Homo sapiens	Q71U36 (AlphaFold model)
Tubulin beta-3 chain	b	protein	450	Homo sapiens	Q13509 (AlphaFold model)

Sequence of entity 1 (a), FASTA

>9WDA_1 Tubulin alpha-1A chain (chains a)
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK
HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA
VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE
AREDMAALEKDYEEVGVDSVEGEGEEEGEEY

Sequence of entity 2 (b), FASTA

>9WDA_2 Tubulin beta-3 chain (chains b)
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPSGNYVGDSDLQLERISVYYNEASSHKYV
PRAILVDLEPGTMDSVRSGAFGHLFRPDNFIFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKECENCDCLQGFQLTHSLGGGTGSGMGTLLISKVREEYPDRIMNTFSVVPSPKVSDTVV
EPYNATLSIHQLVENTDETYCIDNEALYDICFRTLKLATPTYGDLNHLVSATMSGVTTSL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTARGSQQYRALTVPELTQQMFDAKNMM
AACDPRHGRYLTVATVFRGRMSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPPRG
LKMSSTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATAEEEGEMYEDDEEESEAQGPK

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	2
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	1
TA1	Taxol	C47 H51 N O14	1
G2P	Phosphomethylphosphonic acid guanylate ester	C11 H18 N5 O13 P3	1

Primary citation

An evolution-conserved allosteric network in human tubulin governs paclitaxel efficacy. Luo, J., Khoo, C.J., Chen, W. et al. Nat Chem Biol (2026). DOI 10.1038/s41589-026-02204-2 · PubMed

Other PDB entries of the same protein (UniProt Q71U36 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9WD9 2.26 Å, GMPCPP-stabilized human alpha1A/beta3 S239C microtubule
6J8F 2.28 Å, Crystal structure of SVBP-VASH1 with peptide mimic the C-terminal of alpha-tubulin
9WD7 2.34 Å, GMPCPP-stabilizsd human alpha1A/beta3 microtubule
9WDB 2.39 Å, Paclitaxel/GMPCPP-stabilized human alpha1A/beta3 S239C microtubule
22AK 2.41 Å, GDP human alpha1A/beta3 microtubule
22AJ 2.48 Å, GDP human alpha1A/beta3 S239C microtubule
9OX7 2.69 Å, In situ microtubule structure in the axon of a human neuron
8SH7 2.8 Å, TUBB4B and TUBA1A Heterodimer from Human Respiratory Doublet Microtubules
6WSL 3.1 Å, Cryo-EM structure of VASH1-SVBP bound to microtubules
7UNG 3.6 Å, 48-nm repeat of the human respiratory doublet microtubule
5JCO 4.0 Å, Structure and dynamics of single-isoform recombinant neuronal human tubulin
8J07 4.1 Å, 96nm repeat of human respiratory doublet microtubule and associated axonemal complexes

Browse structure collections

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