9YAI: KIF1A R350W

KIF1A R350W bound to microtubules in two-heads-bound state with AMP-PNP. Determined by electron microscopy at 3.12 Å resolution. Released 22 Apr 2026.

Method: Electron microscopy
Resolution: 3.12 Å
Organisms: Homo sapiens, Sus scrofa
Chains: 6
Atoms: 19,749
Mol. weight: 303.77 kDa
Ligands: TA1, GDP, GTP, ANP
Released: 22 Apr 2026

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

Secondary structure: helices and β-sheets

9YAI contains 129 α-helices and 110 β-strands across 6 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, 15 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	14
α-helix	10-27	18
α-helix	37-42	6
β-strand	53-55	3	15
β-strand	61-63	3	15
β-strand	65-68	4	14
β-strand	69	1	16
α-helix	72-79	8
β-strand	93	1	16
α-helix	103-104	2
α-helix	105-109	5
α-helix	115-128	14
β-strand	132-139	8	14
α-helix	144	1
α-helix	145-149	5
α-helix	150-160	11
β-strand	165-171	7	14
α-helix	172-174	3
α-helix	183-189	7
α-helix	191-196	6
β-strand	200-204	5	14
α-helix	206-215	10
α-helix	224-239	16
α-helix	240-242	3
β-strand	248	1	14
α-helix	252-257	6
β-strand	269-272	4	14
α-helix	278-281	4
α-helix	288-295	8
α-helix	298-300	3
β-strand	312-321	10	14
α-helix	325-337	13
β-strand	343	1	14
β-strand	351-356	6	14
α-helix	359-361	3
α-helix	369-370	2
β-strand	373-381	9	14
α-helix	383-399	17
α-helix	405-409	5
α-helix	416-435	20
α-helix	438-439	2

Chain B: 23 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	2-9	8	17
α-helix	10-28	19
β-strand	30	1	18
β-strand	36	1	18
α-helix	42-45	4
α-helix	47-49	3
β-strand	51-53	3	19
β-strand	59-61	3	19
β-strand	63-67	5	17
α-helix	70-77	8
α-helix	87-89	3
β-strand	90-92	3	17
α-helix	101-102	2
α-helix	103-107	5
α-helix	109-124	16
β-strand	129-138	10	17
α-helix	143-158	16
β-strand	163-170	8	17
α-helix	181-195	15
β-strand	198-203	6	17
α-helix	204-209	6
α-helix	210-214	5
α-helix	222-236	15
α-helix	238-241	4
β-strand	246	1	20
α-helix	250-257	8
β-strand	265-266	2	17
β-strand	267-271	5	20
α-helix	286-294	9
α-helix	296-298	3
α-helix	305-307	3
β-strand	310-318	9	20
α-helix	323-336	14
α-helix	338-340	3
β-strand	341	1	20
β-strand	349-354	6	20
β-strand	364-371	8	20
α-helix	374-389	16
α-helix	395-399	5
α-helix	405-426	22

Chain E: 25 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	21
α-helix	10-27	18
α-helix	37-42	6
β-strand	53-55	3	22
β-strand	61-63	3	22
β-strand	65-68	4	21
β-strand	69	1	23
α-helix	73-79	7
β-strand	93	1	23
α-helix	103-104	2
α-helix	105-109	5
α-helix	115-128	14
β-strand	132-140	9	21
α-helix	145-149	5
α-helix	150-160	11
β-strand	165-172	8	21
α-helix	173-174	2
α-helix	183-196	14
β-strand	200-205	6	21
α-helix	206-212	7
α-helix	213-217	5
α-helix	224-239	16
α-helix	240-242	3
β-strand	248	1	24
α-helix	252-259	8
β-strand	269-272	4	24
α-helix	278-281	4
α-helix	288-295	8
α-helix	307-309	3
β-strand	312-321	10	24
α-helix	325-336	12
β-strand	343	1	24
β-strand	351-356	6	24
α-helix	359-361	3
α-helix	369-370	2
β-strand	373-381	9	24
α-helix	384-399	16
α-helix	405-409	5
α-helix	415-434	20
α-helix	438-441	4

Chain I: 23 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	25
α-helix	10-28	19
β-strand	30	1	26
β-strand	35	1	27
β-strand	36	1	26
α-helix	42-45	4
α-helix	47-49	3
β-strand	51-53	3	28
β-strand	58	1	27
β-strand	59-61	3	28
β-strand	63-67	5	25
α-helix	70-77	8
α-helix	87-89	3
β-strand	90-92	3	25
α-helix	101-102	2
α-helix	103-107	5
α-helix	108-126	19
β-strand	130-138	9	25
α-helix	143-158	16
β-strand	163-170	8	25
α-helix	181-192	12
β-strand	198-203	6	25
α-helix	204-209	6
α-helix	210-214	5
α-helix	222-236	15
α-helix	238-241	4
β-strand	246	1	29
α-helix	250-257	8
β-strand	265-266	2	25
β-strand	267-271	5	29
α-helix	276-278	3
α-helix	286-294	9
α-helix	305-307	3
β-strand	310-318	9	29
α-helix	323-336	14
α-helix	338-340	3
β-strand	341	1	29
β-strand	349-354	6	29
β-strand	364-371	8	29
α-helix	374-389	16
α-helix	396-399	4
α-helix	405-426	22

Chain K: 17 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	1
α-helix	6	1
β-strand	7-12	6	2
α-helix	14-16	3
α-helix	17-22	6
β-strand	26	1	3
β-strand	28-31	4	4
β-strand	34-37	4	4
β-strand	49-51	3	4
β-strand	54-57	4	2
α-helix	70-76	7
α-helix	78-86	9
β-strand	91-96	6	2
β-strand	98	1	5
α-helix	103-107	5
β-strand	109	1	6
β-strand	116	1	6
α-helix	118-132	15
β-strand	138-149	12	2
β-strand	154-156	3	2
α-helix	160-162	3
β-strand	166	1	2
β-strand	168-171	4	7
β-strand	175-178	4	7
β-strand	184-186	3	2
α-helix	189-202	14
β-strand	205-206	2	8
β-strand	214-215	2	8
β-strand	218-229	12	2
α-helix	235-236	2
β-strand	240-248	9	2
α-helix	249-251	3
β-strand	252	1	5
α-helix	255-258	4
α-helix	263-290	28
α-helix	310-314	5
α-helix	316-319	4
β-strand	324-330	7	2
β-strand	334	1	3
α-helix	338-353	16
β-strand	355	1	1
α-helix	366-374	9

Chain N: 15 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	6-12	7	9
α-helix	13-15	3
α-helix	17-21	5
β-strand	28-31	4	10
β-strand	34-37	4	10
β-strand	48-51	4	10
β-strand	54-57	4	9
α-helix	70-76	7
α-helix	78-86	9
β-strand	91-96	6	9
α-helix	103-107	5
β-strand	109	1	11
β-strand	116	1	11
α-helix	118-133	16
β-strand	138-150	13	9
β-strand	153-156	4	9
β-strand	166	1	9
α-helix	167	1
β-strand	168-171	4	12
β-strand	175-178	4	12
β-strand	184-185	2	9
α-helix	189-201	13
β-strand	205-206	2	13
β-strand	214-215	2	13
β-strand	218-229	12	9
β-strand	238-248	11	9
α-helix	263-288	26
α-helix	289-294	6
α-helix	310-314	5
α-helix	316-319	4
β-strand	324-331	8	9
α-helix	335-337	3
α-helix	338-350	13
α-helix	364-374	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Kinesin-like protein KIF1A	K, N	protein	438	Homo sapiens	Q12756 (AlphaFold model)
Tubulin alpha-1B chain	A, E	protein	451	Sus scrofa	Q2XVP4 (AlphaFold model)
Tubulin beta-2B chain	B, I	protein	445	Sus scrofa	A0A8D1UIR5 (AlphaFold model)

Sequence of entity 1 (K, N), FASTA

>9YAI_1 Kinesin-like protein KIF1A (chains K, N)
MAGASVKVAVRVRPFNSREMSRDSKCIIQMSGSTTTIVNPKQPKETPKSFSFDYSYWSHT
SPEDINYASQKQVYRDIGEEMLQHAFEGYNVCIFAYGQTGAGKSYTMMGKQEKDQQGIIP
QLCEDLFSRINDTTNDNMSYSVEVSYMEIYCERVRDLLNPKNKGNLRVREHPLLGPYVED
LSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIFTQKRHDAETNITTEK
VSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEMDSGPNKNKKKKK
TDFIPYRDSVLTWLLRENLGGNSRTAMVAALSPADINYDETLSTLRYADWAKQIRCNAVI
NEDPNNKLIRELKDEVTRLRDLLYAQGLGDITDGAGVKQLEDKVEELASKNYHLENEVAR
LKKLVEFTSAWSHPQFEK

Sequence of entity 2 (A, E), FASTA

>9YAI_2 Tubulin alpha-1B chain (chains A, E)
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK
HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA
VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE
AREDMAALEKDYEEVGVDSVEGEGEEEGEEY

Sequence of entity 3 (B, I), FASTA

>9YAI_3 Tubulin beta-2B chain (chains B, I)
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYV
PRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVMPSPKVSDTVV
EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMM
AACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG
LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATADEQGEFEEEEGEDEA

Ligands and cofactors

ID	Name	Formula	Copies
TA1	Taxol	C47 H51 N O14	2
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	2
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	2
ANP	Phosphoaminophosphonic acid-adenylate ester	C10 H17 N6 O12 P3	2
MG	Magnesium ion	Mg	3

Primary citation

Pathogenic KIF1A R350 mutations disrupt a conserved and conformation-dependent kinesin-tubulin salt bridge. Shatarupa, A., Rao, L., Asenjo, A.B. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-71026-6 · PubMed

Other PDB entries of the same protein (UniProt Q12756 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4EJQ 1.89 Å, Crystal structure of KIF1A C-CC1-FHA
4EGX 2.51 Å, Crystal structure of KIF1A CC1-FHA tandem
8UTS 2.7 Å, KIF1A[1-393] APO in complex with a microtubule
9YA5 2.95 Å, KIF1A R350G bound to microtubules in two-heads-bound state with AMP-PNP
8UTU 3.0 Å, KIF1A[1-393] P305L mutant AMP-PNP bound one and two heads bound states merged, in…
8UTV 3.0 Å, KIF1A[1-393] P305L mutant ADP bound in complex with a microtubule
8UTN 3.1 Å, KIF1A[1-393] AMP-PNP bound two-heads-bound state in complex with a microtubule (class…
8UTQ 3.1 Å, KIF1A[1-393] AMP-PNP bound one-head-bound state in complex with a microtubule - class…
8UTT 3.1 Å, KIF1A[1-393] P305L mutant AMP-PNP bound two-heads-bound state in complex with a…
8UTO 3.2 Å, KIF1A[1-393] AMP-PNP bound two-heads-bound state in complex with a microtubule - class…
8UTP 3.2 Å, KIF1A[1-393] - AMP-PNP two-heads-bound state in complex with a microtubule - class T3L1
9YAB 3.21 Å, KIF1A R350W bound to microtubules in the apo state

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