9WD7: Tubulin alpha-1A chain

GMPCPP-stabilizsd human alpha1A/beta3 microtubule. Determined by electron microscopy at 2.34 Å resolution. Released 1 Apr 2026.

Method: Electron microscopy
Resolution: 2.34 Å
Organism: Homo sapiens
Chains: 2
Atoms: 6,795
Mol. weight: 101.76 kDa
Ligands: G2P, MG, GTP
Released: 1 Apr 2026

Explore 9WD7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9WD7 contains 54 α-helices and 33 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: 27 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	1
α-helix	10-28	19
β-strand	35	1	2
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	72-80	9
α-helix	89-91	3
β-strand	92-94	3	1
α-helix	103-104	2
α-helix	105-109	5
α-helix	111-113	3
α-helix	115-126	12
β-strand	132-140	9	1
α-helix	145-149	5
α-helix	150-160	11
β-strand	165-171	7	1
α-helix	172-174	3
α-helix	183-189	7
α-helix	191-196	6
β-strand	200-204	5	1
α-helix	206-215	10
α-helix	224-238	15
α-helix	240-243	4
β-strand	248	1	4
α-helix	252-257	6
β-strand	269-273	5	4
α-helix	280-283	4
α-helix	288-294	7
α-helix	298-300	3
α-helix	307-309	3
β-strand	312-320	9	4
α-helix	325-335	11
β-strand	343	1	4
β-strand	351-356	6	4
α-helix	358-363	6
α-helix	368-370	3
β-strand	374-381	8	4
α-helix	382-384	3
α-helix	385-400	16
α-helix	405-409	5
α-helix	416-434	19

Chain b: 27 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	5
α-helix	10-28	19
β-strand	30	1	6
β-strand	36	1	6
α-helix	42-45	4
α-helix	47-49	3
β-strand	51-53	3	7
β-strand	59-61	3	7
β-strand	63-67	5	5
α-helix	71-77	7
α-helix	82-84	3
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	130-138	9	5
α-helix	143-147	5
α-helix	148-158	11
β-strand	163-170	8	5
α-helix	181-195	15
β-strand	198-203	6	5
α-helix	204-209	6
α-helix	210-214	5
α-helix	222-236	15
α-helix	238-240	3
β-strand	246	1	8
α-helix	250-257	8
β-strand	265-266	2	5
β-strand	267-271	5	8
α-helix	277-281	5
α-helix	286-293	8
α-helix	296-298	3
α-helix	305-307	3
β-strand	310-318	9	8
α-helix	323-336	14
α-helix	338-340	3
β-strand	341	1	8
β-strand	349-354	6	8
β-strand	364-371	8	8
α-helix	372-374	3
α-helix	375-391	17
α-helix	395-399	5
α-helix	406-424	19

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

>9WD7_1 Tubulin alpha-1A chain (chains a)
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK
HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA
VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE
AREDMAALEKDYEEVGVDSVEGEGEEEGEEY

Sequence of entity 2 (b), FASTA

>9WD7_2 Tubulin beta-3 chain (chains b)
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPSGNYVGDSDLQLERISVYYNEASSHKYV
PRAILVDLEPGTMDSVRSGAFGHLFRPDNFIFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKECENCDCLQGFQLTHSLGGGTGSGMGTLLISKVREEYPDRIMNTFSVVPSPKVSDTVV
EPYNATLSIHQLVENTDETYCIDNEALYDICFRTLKLATPTYGDLNHLVSATMSGVTTSL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTARGSQQYRALTVPELTQQMFDAKNMM
AACDPRHGRYLTVATVFRGRMSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPPRG
LKMSSTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATAEEEGEMYEDDEEESEAQGPK

Ligands and cofactors

ID	Name	Formula	Copies
G2P	Phosphomethylphosphonic acid guanylate ester	C11 H18 N5 O13 P3	1
MG	Magnesium ion	Mg	2
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 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
9WDA 2.35 Å, Paclitaxel/GMPCPP-stabilized 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

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