9HQ4: TTLL11

TTLL11 bound to microtubule. Determined by electron microscopy at 3.28 Å resolution. Released 17 Sept 2025.

Method: Electron microscopy
Resolution: 3.28 Å
Organisms: Homo sapiens, Pseudomonas pavonaceae
Chains: 5
Atoms: 17,848
Mol. weight: 315.14 kDa
Ligands: G2P, MG, TA1
Released: 17 Sept 2025

Explore 9HQ4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9HQ4 contains 112 α-helices and 87 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: 21 helices, 15 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	72-79	8
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	145-160	16
β-strand	165-171	7	1
α-helix	172-174	3
α-helix	183-190	8
α-helix	193-196	4
β-strand	200-204	5	1
α-helix	206-215	10
α-helix	224-238	15
α-helix	252-259	8
β-strand	269-272	4	4
α-helix	281-283	3
α-helix	288-296	9
α-helix	307-309	3
β-strand	312-321	10	4
α-helix	325-337	13
β-strand	343	1	4
β-strand	351-356	6	4
α-helix	358-363	6
β-strand	373-381	9	4
α-helix	384-399	16
α-helix	405-409	5
α-helix	416-434	19

Chain B: 23 helices, 22 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
β-strand	51-54	4	7
β-strand	58-61	4	7
β-strand	64-67	4	5
α-helix	70-77	8
α-helix	87-89	3
β-strand	90-92	3	5
α-helix	101-102	2
α-helix	103-107	5
α-helix	110-124	15
β-strand	130-138	9	5
α-helix	143-158	16
β-strand	163-169	7	5
α-helix	170-172	3
α-helix	181-189	9
β-strand	199-201	3	5
α-helix	204-209	6
α-helix	210-214	5
α-helix	222-236	15
α-helix	238-241	4
β-strand	246	1	8
α-helix	250-255	6
β-strand	265-266	2	5
β-strand	267	1	8
β-strand	269	1	9
β-strand	270	1	10
α-helix	279-281	3
α-helix	286-291	6
β-strand	299	1	9
α-helix	305-307	3
β-strand	310-319	10	8
α-helix	323-336	14
β-strand	341	1	8
β-strand	349-354	6	8
α-helix	356-358	3
β-strand	363-364	2	8
β-strand	366	1	10
β-strand	367-371	5	8
α-helix	372-374	3
α-helix	375-389	15
α-helix	395-400	6
α-helix	405-424	20

Chain C: 25 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	5-9	5	11
α-helix	10-28	19
β-strand	35	1	12
α-helix	48-50	3
β-strand	53-55	3	13
β-strand	60	1	12
β-strand	61-63	3	13
β-strand	65-69	5	11
α-helix	76-80	5
α-helix	82-84	3
α-helix	89-91	3
β-strand	92-94	3	11
α-helix	103-104	2
α-helix	105-109	5
α-helix	111-113	3
α-helix	115-126	12
β-strand	134-138	5	11
α-helix	144-159	16
β-strand	165-172	8	11
α-helix	173-174	2
α-helix	183-189	7
α-helix	191-196	6
β-strand	200-205	6	11
α-helix	206-215	10
α-helix	224-238	15
α-helix	240-243	4
β-strand	248	1	14
α-helix	252-259	8
β-strand	269-272	4	14
α-helix	279-281	3
α-helix	288-295	8
α-helix	298-300	3
β-strand	312-321	10	14
α-helix	325-335	11
β-strand	351-356	6	14
α-helix	358-360	3
β-strand	373-381	9	14
α-helix	384-400	17
α-helix	405-410	6
α-helix	415-435	21

Chain D: 22 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	15
α-helix	10-27	18
β-strand	30	1	16
β-strand	36	1	16
α-helix	41-44	4
β-strand	51-53	3	17
α-helix	55-57	3
β-strand	59-61	3	17
β-strand	63-67	5	15
α-helix	70-77	8
α-helix	87-89	3
β-strand	90-92	3	15
α-helix	101-102	2
α-helix	103-107	5
α-helix	110-124	15
β-strand	130-138	9	15
α-helix	143-147	5
α-helix	148-156	9
β-strand	163-169	7	15
α-helix	181-193	13
β-strand	198-202	5	15
α-helix	204-213	10
α-helix	222-236	15
β-strand	244	1	18
α-helix	250-257	8
β-strand	265-266	2	15
β-strand	267-270	4	18
α-helix	286-293	8
α-helix	305-307	3
β-strand	310-319	10	18
α-helix	323-336	14
α-helix	338-340	3
β-strand	341	1	18
β-strand	349-354	6	18
α-helix	357-358	2
β-strand	363-371	9	18
α-helix	374-387	14
α-helix	396-399	4
α-helix	405-426	22

Chain E: 21 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	130-135	6	19
α-helix	137-139	3
α-helix	140-149	10
β-strand	153-155	3	19
β-strand	165-168	4	19
α-helix	172-174	3
β-strand	181-182	2	19
α-helix	188-191	4
α-helix	194-207	14
α-helix	216-217	2
β-strand	218-221	4	20
α-helix	225-238	14
β-strand	246-250	5	20
β-strand	260-262	3	20
α-helix	265-267	3
α-helix	274-276	3
β-strand	279-283	5	20
β-strand	290-291	2	21
β-strand	294-295	2	21
β-strand	296-307	12	22
β-strand	310-315	6	22
β-strand	319-322	4	22
α-helix	345-348	4
β-strand	365-367	3	22
α-helix	368-376	9
α-helix	382-411	30
β-strand	420-421	2	19
β-strand	423-431	9	22
β-strand	437-443	7	22
α-helix	467-483	17
α-helix	486-498	13
α-helix	515-517	3
α-helix	528-530	3
β-strand	532-533	2	22
α-helix	549-558	10
α-helix	570-580	11
α-helix	589-606	18
α-helix	617-630	14
α-helix	639-656	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tubulin alpha-1B chain	A, C	protein	451	Homo sapiens	P68363 (AlphaFold model)
Tubulin beta chain	B, D	protein	444	Homo sapiens	P07437 (AlphaFold model)
Tubulin polyglutamylase TTLL11	E	protein	990	Pseudomonas pavonaceae, Homo sapiens	P0A3G4 (AlphaFold model), Q8NHH1 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>9HQ4_1 Tubulin alpha-1B chain (chains A, C)
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK
HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA
VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE
AREDMAALEKDYEEVGVDSVEGEGEEEGEEY

Sequence of entity 2 (B, D), FASTA

>9HQ4_2 Tubulin beta chain (chains B, D)
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRISVYYNEATGGKYV
PRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVV
EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQVFDAKNMM
AACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG
LKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATAEEEEDFGEEAEEEA

Sequence of entity 3 (E), FASTA

>9HQ4_3 Tubulin polyglutamylase TTLL11 (chains E)
MASAWSHPQFEKGGGSGGGSGGSAWSHPQFEKGGSGGSDYKDDDDKGSGSGEIGTGFPFD
PHYVEVLGERMHYVDVGPRDGTPVLFLHGNPTSSYVWRNIIPHVAPTHRCIAPDLIGMGK
SDKPDLGYFFDDHVRFMDAFIEALGLEEVVLVIHDWGSALGFHWAKRNPERVKGIAFMEF
IRPIPTWDEWPEFARETFQAFRTTDVGRKLIIDQNVFIEGTLPMGVVRPLTEVEMDHYRE
PFLNPVDREPLWRFPNELPIAGEPANIVALVEEYMDWLHQSPVPKLLFWGTPGVLIPPAE
AARLAKSLPNCKAVDIGPGLNLLQEDNPDLIGSEIARWLSTLEISGEPTTEDLYFQSDNA
IASEFCRYPAQWRPLESSRHNQTSLYKKAGSENLYFQSGGGENGSQRPVTVDSSKARTSL
DALKISIRQLKWKEFPFGRRLPCDIYWHGVSFHDNDIFSGQVNKFPGMTEMVRKITLSRA
VRTMQNLFPEEYNFYPRSWILPDEFQLFVAQVQMVKDDDPSWKPTFIVKPDGGCQGDGIY
LIKDPSDIRLAGTLQSRPAVVQEYICKPLLIDKLKFDIRLYVLLKSLDPLEIYIAKDGLS
RFCTEPYQEPTPKNLHRIFMHLTNYSLNIHSGNFIHSDSASTGSKRTFSSILCRLSSKGV
DIKKVWSDIISVVIKTVIALTPELKVFYQSDIPTGRPGPTCFQILGFDILLMKNLKPILL
GVNANPSMRIEHEHELSPGVFENVPSLVDEEVKVAVIRDTLRLMDPLKKKRENQSQQLEK
PFAGKEDALDGELTSAPDCNANPEAHLPSICLKQVFPKYAKQFNYLRLVDRMANLFIRFL
GIKGTMKLGPTGFRTFIRSCKLSSSSLSMAAVDILYIDITRRWNSMTLDQRDSGMCLQAF
VEAFFFLAQRKFKMLPLHEQVASLIDLCEYHLSLLDEKRLVCGRGVPSGGRPPHRGPPQE
PSPSAQPAGDNPPPRTSCANKLSHPRHTLS

Ligands and cofactors

ID	Name	Formula	Copies
G2P	Phosphomethylphosphonic acid guanylate ester	C11 H18 N5 O13 P3	4
MG	Magnesium ion	Mg	4
TA1	Taxol	C47 H51 N O14	2

Primary citation

Mechanistic insights into TTLL11 polyglutamylase-mediated primary tubulin chain elongation. Campbell, J., Vosahlikova, M., Ismail, S. et al. Sci Adv (2025) 11:eadw1561-eadw1561. DOI 10.1126/sciadv.adw1561 · PubMed

Other PDB entries of the same protein (UniProt P68363 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6S8L 1.8 Å, Structure, Thermodynamics, and Kinetics of Plinabulin Binding to two Tubulin Isotypes
6J8O 1.85 Å, Structure of a hypothetical protease
7PJF 1.86 Å, Inhibiting parasite proliferation using a rationally designed anti-tubulin agent
6J4V 2.1 Å, Structural basis of tubulin detyrosination by vasohibins-SVBP enzyme complex and…
8VT7 2.66 Å, Structure of the gamma tubulin ring complex nucleated microtubule protofilament.
7Z6S 2.9 Å, MATCAP bound to a human 14 protofilament microtubule
8V2J 2.9 Å, Structure of alpha1B and betaI/IVb microtubule bound to GDP
9COC 2.9 Å, Two protofilament structure of alpha1B and betaI/IVb microtubule bound to GDP
9BP6 3.1 Å, Structure of alpha1B and betaI/IVb microtubule bound to GMPCPP
9CMM 3.1 Å, Two protofilament structure of alpha1B and betaI/IVb microtubule bound to GMPCPP
7LXB 3.26 Å, HeLa-tubulin in complex with cryptophycin 52
7M18 3.38 Å, HeLa-tubulin in complex with cryptophycin 1

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