9DHZ: HURP

Cryo-EM structure of HURP bound to a microtubule. Determined by electron microscopy at 3.1 Å resolution. Released 16 Jul 2025.

Method: Electron microscopy
Resolution: 3.1 Å
Organisms: Homo sapiens, Sus scrofa
Chains: 5
Atoms: 14,150
Mol. weight: 236.94 kDa
Ligands: MG, GTP, GDP, TA1
Released: 16 Jul 2025

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

Secondary structure: helices and β-sheets

9DHZ contains 97 α-helices and 69 β-strands across 5 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, 19 β-strands

Element	Residues	Length	Sheet
β-strand	2-9	8	1
α-helix	10-28	19
β-strand	30	1	2
β-strand	35	1	3
β-strand	36	1	2
α-helix	42-45	4
α-helix	47-49	3
β-strand	51-53	3	4
β-strand	58	1	3
β-strand	59-61	3	4
β-strand	63-67	5	1
α-helix	71-78	8
α-helix	87-89	3
β-strand	90-92	3	1
α-helix	101-102	2
α-helix	103-107	5
α-helix	109-126	18
β-strand	129-136	8	1
α-helix	142-158	17
β-strand	164-169	6	1
α-helix	170-172	3
α-helix	181-195	15
β-strand	198-202	5	1
α-helix	204-209	6
α-helix	210-214	5
α-helix	222-236	15
α-helix	238-240	3
β-strand	246	1	5
α-helix	250-257	8
β-strand	265-266	2	1
β-strand	267-271	5	5
α-helix	278-281	4
α-helix	286-293	8
α-helix	296-298	3
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	356-358	3
β-strand	364-371	8	5
α-helix	374-390	17
α-helix	395-399	5
α-helix	405-424	20

Chain B: 23 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	2-9	8	6
α-helix	10-27	18
β-strand	35	1	7
α-helix	49-51	3
β-strand	53-56	4	7
β-strand	60-63	4	7
β-strand	65-69	5	6
α-helix	72-79	8
α-helix	89-91	3
β-strand	92-94	3	6
α-helix	103-104	2
α-helix	105-109	5
α-helix	111-128	18
β-strand	131-140	10	6
α-helix	144-160	17
β-strand	165-171	7	6
α-helix	172-174	3
α-helix	183-194	12
α-helix	195-197	3
β-strand	200-204	5	6
α-helix	206-215	10
α-helix	224-243	20
β-strand	248	1	6
α-helix	252-259	8
β-strand	262	1	8
β-strand	265	1	8
β-strand	269-273	5	6
α-helix	278-281	4
α-helix	288-295	8
α-helix	307-309	3
β-strand	312-321	10	6
α-helix	325-337	13
β-strand	343	1	6
β-strand	351-356	6	6
α-helix	358-360	3
α-helix	369-370	2
β-strand	373-381	9	6
α-helix	384-399	16
α-helix	405-409	5
α-helix	416-434	19

Chain C: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	88-115	28
α-helix	125-129	5

Chain K: 24 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	2-9	8	9
α-helix	10-28	19
β-strand	30	1	10
β-strand	36	1	10
α-helix	42-45	4
α-helix	47-49	3
β-strand	51-54	4	11
β-strand	58-61	4	11
β-strand	63-67	5	9
α-helix	70-78	9
α-helix	87-89	3
β-strand	90-92	3	9
α-helix	101-102	2
α-helix	103-107	5
α-helix	109-125	17
β-strand	129-138	10	9
α-helix	143-158	16
β-strand	164-169	6	9
α-helix	170-172	3
α-helix	181-195	15
β-strand	198-202	5	9
α-helix	204-209	6
α-helix	210-214	5
α-helix	222-236	15
α-helix	237-240	4
β-strand	244-246	3	12
α-helix	250-257	8
β-strand	265-266	2	9
β-strand	267-271	5	12
α-helix	286-293	8
α-helix	296-298	3
β-strand	310-319	10	12
α-helix	323-336	14
α-helix	338-340	3
β-strand	341	1	12
β-strand	349-354	6	12
β-strand	363-371	9	12
α-helix	372-374	3
α-helix	375-389	15
α-helix	395-399	5
α-helix	405-424	20

Chain L: 22 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	13
α-helix	10-27	18
α-helix	49-51	3
β-strand	53-56	4	14
β-strand	60-63	4	14
β-strand	65-69	5	13
α-helix	72-80	9
α-helix	89-91	3
β-strand	92-94	3	13
α-helix	103-104	2
α-helix	105-109	5
α-helix	111-127	17
β-strand	132-140	9	13
α-helix	144-160	17
β-strand	165-172	8	13
α-helix	173-174	2
α-helix	183-194	12
β-strand	200-205	6	13
α-helix	206-215	10
α-helix	224-243	20
β-strand	248	1	13
α-helix	252-259	8
β-strand	262	1	15
β-strand	265	1	15
β-strand	269-273	5	13
α-helix	278-281	4
α-helix	288-294	7
α-helix	298-300	3
α-helix	307-309	3
β-strand	312-321	10	13
α-helix	325-337	13
β-strand	343	1	13
β-strand	351-356	6	13
α-helix	359-363	5
β-strand	373-381	9	13
α-helix	384-399	16
α-helix	405-409	5
α-helix	416-435	20

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Disks large-associated protein 5	C	protein	291	Homo sapiens	Q15398 (AlphaFold model)
Tubulin beta chain	A, K	protein	445	Sus scrofa	P02554 (AlphaFold model)
Tubulin alpha-1B chain	B, L	protein	451	Sus scrofa	Q2XVP4 (AlphaFold model)

Sequence of entity 1 (C), FASTA

>9DHZ_1 Disks large-associated protein 5 (chains C)
GSEFELMSSSHFASRHRKDISTEMIRTKIAHRKSLSQKENRHKEYERNRHFGLKDVNIPT
LEGRILVELDETSQGLVPEKTNVKPRAMKTILGDQRKQMLQKYKEEKQLQKLKEQREKAK
RGIFKVGRYRPDMPCFLLSNQNAVKAEPKKAIPSSVRITRSKAKDQMEQTKIDNESDVRA
IRPGPRQTSEKKVSDKEKKVVQPVMPTSLRMTRSATQAAKQVPRTVSSTTARKPVTRAAN
ENEPEGKVPSKGRPAKNVETKPDKGISCKVDSEENTLNSQTNATSGMNPDG

Sequence of entity 2 (A, K), FASTA

>9DHZ_2 Tubulin beta chain (chains A, K)
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYV
PRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVV
EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMM
AACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG
LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATADEQGEFEEEGEEDEA

Sequence of entity 3 (B, L), FASTA

>9DHZ_3 Tubulin alpha-1B chain (chains B, L)
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK
HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA
VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE
AREDMAALEKDYEEVGVDSVEGEGEEEGEEY

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	2
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	2
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	2
TA1	Taxol	C47 H51 N O14	2

Primary citation

HURP regulates Kif18A recruitment and activity to synergistically control microtubule dynamics. Perez-Bertoldi, J.M., Zhao, Y., Thawani, A. et al. Nat Commun (2024) 15:9687-9687. DOI 10.1038/s41467-024-53691-7 · PubMed

Other PDB entries of the same protein (UniProt Q15398 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7ZX4 2.08 Å, Clathrin N-terminal domain in complex with a HURP phospho-peptide
9DUQ 2.8 Å, HURP(65-174) bound to GMPCPP-stabilized microtubule
8X9P 3.54 Å, HURP (428-534)-alpha-tubulin-beta-tubulin complex

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