9DUQ: HURP(65-174)

HURP(65-174) bound to GMPCPP-stabilized microtubule. Determined by electron microscopy at 2.8 Å resolution. Released 27 Nov 2024.

Method: Electron microscopy
Resolution: 2.8 Å
Organisms: Homo sapiens, Sus scrofa
Chains: 27
Atoms: 64,539
Mol. weight: 932.26 kDa
Ligands: GTP, MG, G2P
Released: 27 Nov 2024

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

Secondary structure: helices and β-sheets

9DUQ contains 478 α-helices and 319 β-strands across 27 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, 15 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	6
α-helix	10-28	19
α-helix	49-51	3
β-strand	53	1	7
β-strand	63	1	7
β-strand	65-69	5	6
α-helix	72-80	9
α-helix	89-91	3
β-strand	92-94	3	6
α-helix	103-104	2
α-helix	105-109	5
α-helix	111-113	3
α-helix	115-127	13
β-strand	132-138	7	6
α-helix	144	1
α-helix	145-149	5
α-helix	150-160	11
β-strand	165-172	8	6
α-helix	173-174	2
α-helix	183-197	15
β-strand	200-205	6	6
α-helix	206-215	10
α-helix	224-243	20
α-helix	252-259	8
β-strand	262	1	8
β-strand	265	1	8
α-helix	268	1
β-strand	269-273	5	6
α-helix	278-281	4
α-helix	288-295	8
α-helix	298-300	3
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	359-361	3
α-helix	369-370	2
β-strand	373-381	9	6
α-helix	384-400	17
α-helix	406-409	4
α-helix	415-436	22

Chain B: 25 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	1
α-helix	10-27	18
β-strand	30	1	2
β-strand	35	1	3
β-strand	36	1	2
α-helix	42-47	4
α-helix	49-51	3
β-strand	53-55	3	4
β-strand	60	1	3
β-strand	61-63	3	4
β-strand	65-69	5	1
α-helix	72-80	9
β-strand	92-94	3	1
α-helix	103-104	2
α-helix	105-109	5
α-helix	111-127	17
β-strand	132-140	9	1
α-helix	145-149	5
α-helix	150-160	11
β-strand	165-172	8	1
α-helix	173	1
α-helix	183-194	12
β-strand	200-202	3	1
β-strand	204-205	2	1
α-helix	206-211	6
α-helix	212-216	5
α-helix	224-237	14
α-helix	240-243	4
β-strand	248	1	5
α-helix	252-259	8
β-strand	267-268	2	1
β-strand	269-273	5	5
α-helix	288-296	9
α-helix	298-300	3
α-helix	307-309	3
β-strand	312-321	10	5
α-helix	325-338	14
α-helix	340-342	3
β-strand	343	1	5
β-strand	351-356	6	5
α-helix	359-360	2
β-strand	373-381	9	5
α-helix	384-400	17
α-helix	405-410	6
α-helix	415-436	22

Chain C: 23 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	13
α-helix	10-28	19
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	72-79	8
α-helix	89-91	3
β-strand	92-94	3	13
α-helix	103-104	2
α-helix	105-109	5
α-helix	115-126	12
β-strand	132-138	7	13
α-helix	144	1
α-helix	145-149	5
α-helix	150-160	11
β-strand	165-172	8	13
α-helix	173-174	2
α-helix	183-197	15
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	279-282	4
α-helix	288-295	8
α-helix	298-300	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	359-361	3
β-strand	373-381	9	13
α-helix	384-400	17
α-helix	405-409	5
α-helix	415-436	22

Chain D: 26 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	9
α-helix	10-28	19
β-strand	30	1	10
β-strand	35	1	11
β-strand	36	1	10
α-helix	41-43	3
β-strand	53-56	4	11
β-strand	60-63	4	11
β-strand	65-69	5	9
α-helix	72-80	9
α-helix	89-91	3
β-strand	92-94	3	9
α-helix	103-104	2
α-helix	105-109	5
α-helix	112-128	17
β-strand	132-140	9	9
α-helix	145-149	5
α-helix	150-160	11
β-strand	165-171	7	9
α-helix	183-197	15
β-strand	200-204	5	9
α-helix	206-211	6
α-helix	212-216	5
α-helix	224-238	15
α-helix	240-243	4
β-strand	248	1	12
α-helix	252-259	8
β-strand	267-268	2	9
β-strand	269-273	5	12
α-helix	281-283	3
α-helix	288-295	8
α-helix	298-300	3
α-helix	307-309	3
β-strand	312-321	10	12
α-helix	325-338	14
α-helix	340-342	3
β-strand	343	1	12
β-strand	351-356	6	12
α-helix	359-360	2
β-strand	373-381	9	12
α-helix	382-384	3
α-helix	385-399	15
α-helix	405-409	5
α-helix	415-436	22

Chain E: 24 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	19
α-helix	10-28	19
β-strand	35	1	20
α-helix	48-51	4
β-strand	53-56	4	20
β-strand	60-63	4	20
β-strand	65-69	5	19
α-helix	73-80	8
α-helix	89-91	3
β-strand	92-94	3	19
α-helix	103-104	2
α-helix	105-109	5
α-helix	110-126	17
β-strand	134-140	7	19
α-helix	144	1
α-helix	145-149	5
α-helix	150-160	11
β-strand	165-172	8	19
α-helix	173-174	2
α-helix	183-197	15
β-strand	200-205	6	19
α-helix	206-215	10
α-helix	224-243	20
β-strand	248	1	19
α-helix	252-259	8
β-strand	262	1	21
β-strand	265	1	21
β-strand	269-273	5	19
α-helix	278-281	4
α-helix	288-295	8
α-helix	298-300	3
α-helix	307-309	3
β-strand	312-320	9	19
α-helix	325-337	13
β-strand	343	1	19
β-strand	351-356	6	19
α-helix	358-361	4
β-strand	374-381	8	19
α-helix	384-400	17
α-helix	405-409	5
α-helix	415-435	21

Chain F: 24 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	16
α-helix	10-28	19
β-strand	30	1	17
β-strand	35	1	18
β-strand	36	1	17
α-helix	42-47	4
α-helix	49-51	3
β-strand	53-56	4	18
β-strand	60-63	4	18
β-strand	65-69	5	16
α-helix	72-80	9
α-helix	84-86	3
α-helix	89-91	3
β-strand	92-94	3	16
α-helix	103-104	2
α-helix	105-109	5
α-helix	111-128	18
β-strand	132-140	9	16
α-helix	145-149	5
α-helix	150-160	11
β-strand	165-172	8	16
α-helix	183-197	15
β-strand	200-205	6	16
α-helix	206-211	6
α-helix	212-216	5
α-helix	224-243	20
β-strand	248	1	16
α-helix	252-259	8
β-strand	267-273	7	16
α-helix	281-283	3
α-helix	288-295	8
α-helix	307-309	3
β-strand	312-321	10	16
α-helix	325-338	14
β-strand	343	1	16
β-strand	351-356	6	16
α-helix	359-360	2
β-strand	373-381	9	16
α-helix	384-400	17
α-helix	405-410	6
α-helix	415-436	22

Chain G: 27 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	26
α-helix	10-28	19
α-helix	48-51	4
β-strand	53-56	4	27
β-strand	60-63	4	27
β-strand	65-69	5	26
α-helix	72-80	9
α-helix	89-91	3
β-strand	92-94	3	26
α-helix	103-104	2
α-helix	105-109	5
α-helix	112-126	15
β-strand	132-140	9	26
α-helix	144	1
α-helix	145-149	5
α-helix	150-160	11
β-strand	165-171	7	26
β-strand	172	1	28
α-helix	173-174	2
α-helix	183-197	15
β-strand	200-202	3	26
β-strand	203	1	29
β-strand	205	1	28
α-helix	206-215	10
α-helix	224-243	20
β-strand	248	1	29
α-helix	252-259	8
β-strand	262	1	30
β-strand	265	1	30
β-strand	269-273	5	29
α-helix	278-283	6
α-helix	288-294	7
α-helix	298-300	3
β-strand	301	1	29
α-helix	307-309	3
β-strand	312-321	10	29
α-helix	325-336	12
α-helix	342	1
β-strand	343	1	29
α-helix	344	1
β-strand	351-356	6	29
α-helix	359-361	3
β-strand	373-381	9	29
α-helix	382-384	3
α-helix	385-399	15
α-helix	405-409	5
α-helix	416-436	21

Chain H: 24 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	22
α-helix	10-27	18
β-strand	30	1	23
β-strand	35	1	24
β-strand	36	1	23
α-helix	41-43	3
α-helix	49-51	3
β-strand	53-56	4	24
β-strand	60-63	4	24
β-strand	65-69	5	22
α-helix	72-80	9
α-helix	89-91	3
β-strand	92-94	3	22
α-helix	103-104	2
α-helix	105-109	5
α-helix	111-128	18
β-strand	132-140	9	22
α-helix	145-160	16
β-strand	165-171	7	22
α-helix	183-194	12
β-strand	200-204	5	22
α-helix	206-211	6
α-helix	212-216	5
α-helix	224-237	14
α-helix	240-243	4
β-strand	246-248	3	25
α-helix	252-259	8
β-strand	267-268	2	22
β-strand	269-273	5	25
α-helix	288-296	9
α-helix	298-300	3
α-helix	307-309	3
β-strand	312-321	10	25
α-helix	325-338	14
α-helix	340-342	3
β-strand	343	1	25
β-strand	351-356	6	25
α-helix	359-360	2
β-strand	373-381	9	25
α-helix	384-400	17
α-helix	405-409	5
α-helix	415-436	22

11 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Disks large-associated protein 5	r, s, t, u, v, w, x, y, z	protein	46	Homo sapiens	Q15398 (AlphaFold model)
Tubulin beta chain	B, D, F, H, J, L, N, P, R	protein	427	Sus scrofa	P02554 (AlphaFold model)
Tubulin alpha chain	A, C, E, G, I, K, M, O, Q	protein	439	Sus scrofa	Q2XVP4 (AlphaFold model)

Sequence of entity 1 (r, s, t, u, v, w, x, y, z), FASTA

>9DUQ_1 Disks large-associated protein 5 (chains r, s, t, u, v, w, x, y, z)
GDQRKQMLQKYKEEKQLQKLKEQREKAKRGIFKVGRYRPDMPCFLL

Sequence of entity 2 (B, D, F, H, J, L, N, P, R), FASTA

>9DUQ_2 Tubulin beta chain (chains B, D, F, H, J, L, N, P, R)
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYV
PRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVV
EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMM
AACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG
LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQD

Sequence of entity 3 (A, C, E, G, I, K, M, O, Q), FASTA

>9DUQ_3 Tubulin alpha chain (chains A, C, E, G, I, K, M, O, Q)
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK
HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA
VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE
AREDMAALEKDYEEVGVDS

Ligands and cofactors

ID	Name	Formula	Copies
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	9
MG	Magnesium ion	Mg	18
G2P	Phosphomethylphosphonic acid guanylate ester	C11 H18 N5 O13 P3	9

Primary citation

HURP facilitates spindle assembly by stabilizing microtubules and working synergistically with TPX2. Valdez, V.A., Ma, M., Gouveia, B. et al. Nat Commun (2024) 15:9689-9689. DOI 10.1038/s41467-024-53630-6 · 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
9DHZ 3.1 Å, Cryo-EM structure of HURP bound to a microtubule
8X9P 3.54 Å, HURP (428-534)-alpha-tubulin-beta-tubulin complex

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