7TR2: Apo CaKip3[2-436]-L2-mutant(HsKHC)

Apo CaKip3[2-436]-L2-mutant(HsKHC) in complex with a microtubule. Determined by electron microscopy at 3.0 Å resolution. Released 13 Jul 2022.

Method: Electron microscopy
Resolution: 3.0 Å
Organisms: Candida albicans, Homo sapiens, Sus scrofa
Chains: 3
Atoms: 9,586
Mol. weight: 148.39 kDa
Ligands: GDP, TA1, MG, GTP
Released: 13 Jul 2022

Explore 7TR2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7TR2 contains 65 α-helices and 50 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: 28 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	5
α-helix	10-28	19
α-helix	37-41	5
β-strand	53-55	3	6
β-strand	61-63	3	6
β-strand	65-69	5	5
α-helix	73-79	7
β-strand	92-93	2	5
α-helix	103-104	2
α-helix	105-109	5
α-helix	111-113	3
α-helix	115-127	13
β-strand	134-140	7	5
α-helix	144	1
α-helix	145-149	5
α-helix	150-160	11
β-strand	165-171	7	5
α-helix	172-174	3
α-helix	183-189	7
α-helix	191-196	6
β-strand	200-204	5	5
α-helix	206-212	7
α-helix	213-217	5
α-helix	224-238	15
α-helix	240-242	3
β-strand	248	1	7
α-helix	252-259	8
β-strand	262	1	8
β-strand	265	1	8
β-strand	269-272	4	7
α-helix	278-281	4
α-helix	288-295	8
α-helix	307-309	3
β-strand	312-321	10	7
α-helix	325-337	13
β-strand	343	1	7
β-strand	351-356	6	7
α-helix	359-361	3
α-helix	369-370	2
β-strand	373-381	9	7
α-helix	384-399	16
α-helix	405-409	5
α-helix	416-435	20
α-helix	438-439	2

Chain B: 24 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	9
α-helix	10-28	19
β-strand	30	1	10
β-strand	36	1	10
α-helix	41-45	5
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	70-77	8
α-helix	82-84	3
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	130-138	9	9
α-helix	143-158	16
β-strand	163-170	8	9
α-helix	181-192	12
β-strand	198-199	2	9
β-strand	200	1	12
β-strand	202-203	2	9
α-helix	204-209	6
α-helix	210-214	5
α-helix	222-236	15
α-helix	238-241	4
β-strand	244-246	3	13
α-helix	250-257	8
β-strand	266	1	12
β-strand	267-270	4	13
α-helix	286-293	8
α-helix	296-298	3
α-helix	305-307	3
β-strand	310-318	9	13
α-helix	323-336	14
α-helix	338-340	3
β-strand	341	1	13
β-strand	349-354	6	13
β-strand	364-371	8	13
α-helix	374-389	16
α-helix	395-400	6
α-helix	405-426	22

Chain K: 13 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	26-32	7	1
α-helix	33-36	4
α-helix	37-50	14
β-strand	113-114	2	2
β-strand	146-147	2	2
β-strand	150-152	3	1
α-helix	158-165	8
α-helix	167-175	9
β-strand	179-184	6	1
α-helix	191-195	5
β-strand	197	1	3
β-strand	202	1	3
α-helix	204-219	16
β-strand	223-235	13	1
β-strand	238-241	4	1
β-strand	270	1	1
α-helix	275-288	14
β-strand	291-294	4	4
β-strand	297-301	5	4
β-strand	304-315	12	1
β-strand	327-333	7	1
α-helix	334-337	4
α-helix	348-371	24
α-helix	373-377	5
α-helix	381-383	3
α-helix	385-389	5
β-strand	399-406	8	1
α-helix	413-426	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Kinesin-like protein,Kinesin-1 heavy chain	K	protein	420	Candida albicans, Homo sapiens	C4YNU9 (AlphaFold model), P33176 (AlphaFold model)
Tubulin alpha-1B chain	A	protein	451	Sus scrofa	Q2XVP4 (AlphaFold model)
Tubulin beta-2B chain	B	protein	445	Sus scrofa	P02554 (AlphaFold model)

Sequence of entity 1 (K), FASTA

>7TR2_1 Kinesin-like protein,Kinesin-1 heavy chain (chains K)
MASYPNSLGSPATVTSTSVPTAKQSSISVAVRVRPFTEAESNRLVKIDNDDVFLGDGCLT
SDNNNNNNNSNSNGNGNGNGSSAANSSGASTSRRAIFNTLGGLRKIINVVDDRMLIIASK
RFVFDRLFDEDCTQDQVYRNTTQPLLDSVLDGYNATVFAYGATGCGKTHTISGTPEDPGV
IFLTMKELYNRIEELKDTKIIDISLSYLEIYNETIRDLLNPMTQCKNLVIREDANNKISV
SNLSRHRPNSVEEVMQLILEGNKNRTCSPTEANATSSRSHAVLQINVIQKDRTGDITEEH
TFATLSIIDLAGSERAAATKNRGARLNEGANINKSLLALGNCINALCDPRRRNHVPYRDS
KLTRLLKFSLGGNCKTVMIVCVSPSSQHYDETLNTLKYADRAKEIKTKLIRNLEHHHHHH

Sequence of entity 2 (A), FASTA

>7TR2_2 Tubulin alpha-1B chain (chains A)
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK
HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA
VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE
AREDMAALEKDYEEVGVDSVEGEGEEEGEEY

Sequence of entity 3 (B), FASTA

>7TR2_3 Tubulin beta-2B chain (chains B)
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYV
PRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVMPSPKVSDTVV
EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMM
AACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG
LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATADEQGEFEEEEGEDEA

Ligands and cofactors

ID	Name	Formula	Copies
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	1
TA1	Taxol	C47 H51 N O14	1
MG	Magnesium ion	Mg	1
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	1

Primary citation

Kinesin-8-specific loop-2 controls the dual activities of the motor domain according to tubulin protofilament shape. Hunter, B., Benoit, M.P.M.H., Asenjo, A.B. et al. Nat Commun (2022) 13:4198-4198. DOI 10.1038/s41467-022-31794-3 · PubMed

Other PDB entries of the same protein (UniProt C4YNU9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7TR1 3.1 Å, CaKip3[2-436]-L2-mutant(HsKHC) - AMP-PNP in complex with a microtubule

Browse structure collections

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