7TR1: CaKip3[2-436]-L2-mutant(HsKHC) - AMP-PNP

CaKip3[2-436]-L2-mutant(HsKHC) - AMP-PNP in complex with a microtubule. Determined by electron microscopy at 3.1 Å resolution. Released 20 Jul 2022.

Method: Electron microscopy
Resolution: 3.1 Å
Organisms: Candida albicans, Homo sapiens, Sus scrofa
Chains: 3
Atoms: 9,707
Mol. weight: 148.92 kDa
Ligands: TA1, GDP, GTP, ANP
Released: 20 Jul 2022

Explore 7TR1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7TR1 contains 67 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: 24 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	5-9	5	7
α-helix	10-28	19
α-helix	37-40	4
β-strand	53-55	3	8
β-strand	61-63	3	8
β-strand	65-69	5	7
α-helix	75-80	6
β-strand	92-93	2	7
α-helix	103-104	2
α-helix	105-109	5
α-helix	111-113	3
α-helix	115-128	14
β-strand	134-139	6	7
α-helix	144-160	17
β-strand	165-172	8	7
α-helix	173-174	2
α-helix	183-193	11
β-strand	200-205	6	7
α-helix	206-212	7
α-helix	213-217	5
α-helix	224-243	20
β-strand	248	1	9
α-helix	253-259	7
β-strand	269-272	4	7
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	7
α-helix	325-337	13
β-strand	343	1	7
β-strand	351-354	4	7
β-strand	355	1	9
α-helix	359-360	2
β-strand	373-381	9	7
α-helix	384-401	18
α-helix	406-410	5
α-helix	416-434	19
α-helix	438-439	2

Chain B: 27 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	10
α-helix	10-28	19
β-strand	30	1	11
β-strand	36	1	11
α-helix	42-45	4
α-helix	47-49	3
β-strand	51-53	3	12
β-strand	59-61	3	12
β-strand	63-67	5	10
α-helix	71-78	8
α-helix	87-89	3
β-strand	90-92	3	10
α-helix	101-102	2
α-helix	103-107	5
α-helix	109-111	3
α-helix	113-125	13
β-strand	130-138	9	10
α-helix	143	1
α-helix	144-148	5
α-helix	149-158	10
β-strand	163-170	8	10
α-helix	171-172	2
α-helix	181-195	15
β-strand	198-203	6	10
α-helix	204-209	6
α-helix	210-214	5
α-helix	222-233	12
α-helix	238-240	3
β-strand	246	1	13
α-helix	250-255	6
β-strand	265-266	2	10
β-strand	267-271	5	13
α-helix	286-294	9
α-helix	296-298	3
α-helix	305-307	3
β-strand	310-319	10	13
α-helix	323-336	14
α-helix	338-340	3
β-strand	341	1	13
β-strand	349-354	6	13
β-strand	363-371	9	13
α-helix	374-389	16
α-helix	396-399	4
α-helix	405-426	22

Chain K: 16 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	23-25	3	1
β-strand	27-32	6	2
α-helix	33-35	3
α-helix	37-42	6
α-helix	43-47	5
α-helix	48-50	3
β-strand	113-115	3	3
β-strand	145-147	3	3
α-helix	158-165	8
α-helix	167-174	8
β-strand	178-185	8	2
α-helix	192-195	4
β-strand	197	1	4
β-strand	202	1	4
α-helix	204-219	16
β-strand	224-235	12	2
β-strand	238-241	4	2
β-strand	254-256	3	5
β-strand	262-264	3	5
β-strand	270	1	2
α-helix	275-288	14
β-strand	291	1	6
β-strand	301	1	6
β-strand	304-314	11	2
β-strand	327-333	7	2
α-helix	340-342	3
α-helix	348-371	24
α-helix	381-383	3
α-helix	385-389	5
α-helix	391	1
α-helix	392-396	5
β-strand	399-406	8	2
α-helix	414-426	13
β-strand	430-432	3	1

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

>7TR1_1 Kinesin-like protein,Kinesin-1 heavy chain (chains K)
MASYPNSLGSPATVTSTSVPTAKQSSISVAVRVRPFTEAESNRLVKIDNDDVFLGDGCLT
SDNNNNNNNSNSNGNGNGNGSSAANSSGASTSRRAIFNTLGGLRKIINVVDDRMLIIASK
RFVFDRLFDEDCTQDQVYRNTTQPLLDSVLDGYNATVFAYGATGCGKTHTISGTPEDPGV
IFLTMKELYNRIEELKDTKIIDISLSYLEIYNETIRDLLNPMTQCKNLVIREDANNKISV
SNLSRHRPNSVEEVMQLILEGNKNRTCSPTEANATSSRSHAVLQINVIQKDRTGDITEEH
TFATLSIIDLAGSERAAATKNRGARLNEGANINKSLLALGNCINALCDPRRRNHVPYRDS
KLTRLLKFSLGGNCKTVMIVCVSPSSQHYDETLNTLKYADRAKEIKTKLIRNLEHHHHHH

Sequence of entity 2 (A), FASTA

>7TR1_2 Tubulin alpha-1B chain (chains A)
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK
HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA
VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE
AREDMAALEKDYEEVGVDSVEGEGEEEGEEY

Sequence of entity 3 (B), FASTA

>7TR1_3 Tubulin beta-2B chain (chains B)
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYV
PRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVMPSPKVSDTVV
EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMM
AACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG
LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATADEQGEFEEEEGEDEA

Ligands and cofactors

ID	Name	Formula	Copies
TA1	Taxol	C47 H51 N O14	1
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	1
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	1
ANP	Phosphoaminophosphonic acid-adenylate ester	C10 H17 N6 O12 P3	1
MG	Magnesium ion	Mg	2

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:

7TR2 3.0 Å, Apo CaKip3[2-436]-L2-mutant(HsKHC) in complex with a microtubule

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