8X9P: Tubulin alpha chain

HURP (428-534)-alpha-tubulin-beta-tubulin complex. Determined by electron microscopy at 3.54 Å resolution. Released 23 Oct 2024.

Method: Electron microscopy
Resolution: 3.54 Å
Organisms: Bos taurus, Homo sapiens
Chains: 3
Atoms: 7,669
Mol. weight: 172.88 kDa
Released: 23 Oct 2024

Explore 8X9P in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8X9P contains 52 α-helices and 33 β-strands across 3 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: 23 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	1
α-helix	11-28	18
β-strand	53-55	3	2
β-strand	61-63	3	2
β-strand	65-69	5	1
α-helix	72-79	8
α-helix	84-86	3
β-strand	92-94	3	1
α-helix	103-104	2
α-helix	105-109	5
α-helix	112-127	16
β-strand	134-140	7	1
α-helix	144-161	18
β-strand	165-172	8	1
α-helix	175-177	3
α-helix	183-194	12
β-strand	200-205	6	1
α-helix	206-215	10
α-helix	224-243	20
α-helix	252-259	8
β-strand	269-273	5	3
β-strand	277	1	4
α-helix	278-280	3
α-helix	284-286	3
α-helix	288-296	9
β-strand	301	1	3
α-helix	307-309	3
β-strand	312-321	10	3
α-helix	325-338	14
β-strand	343	1	3
β-strand	351-356	6	3
α-helix	359-361	3
β-strand	368	1	4
α-helix	369-370	2
β-strand	373-381	9	3
α-helix	382-384	3
α-helix	385-399	15
α-helix	405-410	6
α-helix	416-437	22

Chain B: 24 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	5
α-helix	11-27	17
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	70-77	8
α-helix	87-89	3
β-strand	91-92	2	5
α-helix	101-102	2
α-helix	103-107	5
α-helix	110-126	17
β-strand	130-138	9	5
α-helix	142-158	17
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	222-241	20
α-helix	250-257	8
β-strand	265-266	2	5
β-strand	267-271	5	8
α-helix	286-293	8
α-helix	296-298	3
β-strand	299	1	8
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	351-354	4	8
α-helix	357-358	2
β-strand	364-371	8	8
α-helix	372-374	3
α-helix	375-390	16
α-helix	396-399	4
α-helix	405-426	22

Chain C: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	231-255	25
α-helix	262-277	16
α-helix	278-283	6
α-helix	284-295	12
α-helix	304-333	30

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tubulin alpha chain	A	protein	439	Bos taurus	P02550 (AlphaFold model)
Tubulin beta chain	B	protein	427	Bos taurus	P02554 (AlphaFold model)
Disks large-associated protein 5,Green fluorescent protein	C	protein	675	Homo sapiens	P42212 (AlphaFold model), Q15398 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>8X9P_1 Tubulin alpha chain (chains A)
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK
HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFSVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA
VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRGHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYEPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE
AREDMAALEKDYEEVGVDS

Sequence of entity 2 (B), FASTA

>8X9P_2 Tubulin beta chain (chains B)
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYV
PRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVV
EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMM
AACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG
LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQD

Sequence of entity 3 (C), FASTA

>8X9P_3 Disks large-associated protein 5,Green fluorescent protein (chains C)
MGSSHHHHHHSQDPNSDYDIPTTENLYFQGAAAMPTSLRMTRSATQAAKQVPRTVSSTTA
RKPVTRAANENEPEGKVPSKGRPAKNVETKPDKGISCKVDSEENTLNSQTNATSGMNPDG
VLSKMENLPEINTAKIKGKNSFAPKDFMFQPLDGLKTYQVTPMTPRSANAFLTPSYTWTP
LKTEVDESQATKEILAQKCKTYSTKTIQQDSNKLPCPLGPLTVWHEEHVLNKNEATTKNL
NGLPIKEVPSLERNEGRIAQPHHGVPYFRNILQSETEKLTSHCFEWDRKLELDIPDDAKD
LIRTAVGQTRLLMKERFKQFEGLVDDCEYKRGIKETTCTDLDGFWDMVSFQIEDVIHKFN
NLIKLEESGWQVNNNMNHNMNKNVFRKKVVSGIASKPKQDDAGRIAARNRLAAIKNAMRE
RIRQEECAETAVSVIPKEVDKIVFDAGFFRVESPLEGMVSKGEELFTGVVPILVELDGDV
NGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKQHD
FFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLE
YNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLS
TQSALSKDPNEKRDH

Primary citation

HURP binding to the vinca domain of beta-tubulin accounts for cancer drug resistance. Saju, A., Chen, P.P., Weng, T.H. et al. Nat Commun (2024) 15:8844-8844. DOI 10.1038/s41467-024-53139-y · PubMed

Other PDB entries of the same protein (UniProt P02550 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7X4N 2.88 Å, Crystal Structure of C. elegans kinesin-4 KLP-12 complexed with tubulin and DARPin
9T1D 2.9 Å, Cryo-EM reconstruction of undecorated GDP microtubule
6MZG 3.21 Å, Structural Basis of Tubulin Recruitment and Assembly by Microtubule Polymerases with…
7U0F 3.53 Å, HIV-1 Rev in complex with tubulin
8QAU 3.54 Å, Outer kinetochore Ndc80-Dam1 alpha/beta-tubulin complex
6MZE 3.6 Å, Structural Basis of Tubulin Recruitment and Assembly by Microtubule Polymerases with…
6KIQ 3.62 Å, Complex of yeast cytoplasmic dynein MTBD-High and MT with DTT
1TUB 3.7 Å, Tubulin alpha-beta dimer, electron diffraction
9EDT 3.7 Å, Tubulin cofactors D,E,G bound to tubulin dimer
9EEB 3.7 Å, Tubulin cofactors D,E,G bound to tubulin dimer
9EDR 3.8 Å, Tubulin Cofactors D,E,G,C and Tubulin complex -- TBCC N Terminus Bound to Tubulin
9EDS 3.8 Å, Tubulin cofactors D,E,G,C bound to tubulin dimer -- TBCC N terminus unbound

Browse structure collections

About this viewer

MolViewer shows 8X9P directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.