2Y65: Kinesin heavy chain

Crystal structure of Drosophila melanogaster kinesin-1 motor domain dimer-tail complex. Determined by X-ray diffraction at 2.2 Å resolution. Released 24 Aug 2011.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: DROSOPHILA MELANOGASTER
Chains: 7
Atoms: 11,750
Mol. weight: 171.09 kDa
Ligands: MG, ADP
Released: 24 Aug 2011

Explore 2Y65 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2Y65 contains 71 α-helices and 92 β-strands across 7 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: 19 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	10-12	3	1
α-helix	13	1
β-strand	14-19	6	2
α-helix	20-22	3
α-helix	24-28	5
β-strand	33	1	3
β-strand	35-36	2	4
β-strand	45-48	4	4
β-strand	51-54	4	4
β-strand	57-59	3	2
α-helix	65-68	4
α-helix	69-73	5
α-helix	74-81	8
β-strand	86-91	6	2
α-helix	98-102	5
β-strand	104	1	5
β-strand	112	1	5
α-helix	114-128	15
β-strand	133-145	13	2
β-strand	148-151	4	2
β-strand	160	1	2
α-helix	161	1
β-strand	162-164	3	6
β-strand	170-172	3	6
β-strand	178-180	3	2
α-helix	183-197	15
α-helix	204-209	6
β-strand	212-223	12	2
β-strand	229-238	10	2
α-helix	239-241	3
α-helix	263-277	15
α-helix	285-287	3
α-helix	289-293	5
α-helix	295-297	3
β-strand	303-310	8	2
β-strand	313	1	3
α-helix	314-316	3
α-helix	317-330	14
β-strand	334-336	3	1
β-strand	340-342	3	2
α-helix	346-350	5

Chain B: 16 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	10-12	3	7
α-helix	13	1
β-strand	14-19	6	8
α-helix	20-22	3
α-helix	24-28	5
β-strand	33	1	9
β-strand	35-36	2	10
β-strand	45-48	4	10
β-strand	51-54	4	10
β-strand	57-59	3	8
α-helix	65-72	8
α-helix	74-81	8
β-strand	86-91	6	8
α-helix	98-102	5
β-strand	104	1	11
β-strand	112	1	11
α-helix	114-127	14
β-strand	133-145	13	8
β-strand	148-151	4	8
β-strand	154	1	8
β-strand	161-164	4	12
β-strand	170-173	4	12
β-strand	178-180	3	8
α-helix	183-197	15
α-helix	204-208	5
β-strand	212-223	12	8
β-strand	228-238	11	8
α-helix	239-241	3
α-helix	263-277	15
α-helix	285-287	3
α-helix	289-293	5
β-strand	303-310	8	8
β-strand	313	1	9
α-helix	314-316	3
α-helix	317-330	14
β-strand	334-336	3	7
β-strand	340-343	4	8
α-helix	345-360	16

Chain C: 18 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	10-12	3	13
α-helix	13	1
β-strand	14-19	6	14
α-helix	20-22	3
α-helix	24-28	5
β-strand	33	1	15
β-strand	35-36	2	16
β-strand	45-48	4	16
β-strand	51-54	4	16
β-strand	57-59	3	14
α-helix	65-68	4
α-helix	69-73	5
α-helix	75-81	7
β-strand	86-91	6	14
α-helix	98-102	5
β-strand	104	1	17
β-strand	112	1	17
α-helix	114-127	14
β-strand	133-145	13	14
β-strand	148-151	4	14
β-strand	158-160	3	14
α-helix	161	1
β-strand	162-164	3	18
β-strand	170-172	3	18
β-strand	178-180	3	14
α-helix	183-197	15
α-helix	204-209	6
β-strand	211-223	13	14
β-strand	229-238	10	14
α-helix	239-241	3
α-helix	263-277	15
α-helix	285-287	3
α-helix	289-293	5
β-strand	303-310	8	14
β-strand	313	1	15
α-helix	314-316	3
α-helix	317-330	14
β-strand	334-336	3	13
β-strand	340-342	3	14
α-helix	345-362	18

Chain D: 17 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	11-12	2	19
α-helix	13	1
β-strand	14-19	6	20
α-helix	20-23	4
α-helix	24-29	6
β-strand	33	1	21
β-strand	36	1	22
β-strand	45-48	4	22
β-strand	51-54	4	22
β-strand	57-59	3	20
α-helix	65-72	8
α-helix	74-80	7
β-strand	86-91	6	20
α-helix	98-102	5
β-strand	104	1	23
β-strand	112	1	23
α-helix	114-128	15
β-strand	133-145	13	20
β-strand	148-151	4	20
β-strand	158-160	3	20
β-strand	162-163	2	24
β-strand	171-172	2	24
β-strand	178-179	2	20
α-helix	183-196	14
α-helix	204-210	7
β-strand	212-223	12	20
β-strand	229-238	10	20
α-helix	239-241	3
α-helix	263-277	15
α-helix	285-287	3
α-helix	289-293	5
β-strand	303-310	8	20
β-strand	313	1	21
α-helix	314-316	3
α-helix	317-330	14
β-strand	334-335	2	19
β-strand	340-342	3	20
α-helix	343-344	2
α-helix	345-361	17

Chain W: 0 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	941-942	2	14
β-strand	946	1	20

Chain X: 1 helix, 1 β-strand

Element	Residues	Length	Sheet
α-helix	939-940	2
β-strand	941-942	2	8

Chain Y: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	941-942	2	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Kinesin heavy chain	A, B, C, D	protein	365	DROSOPHILA MELANOGASTER	P17210 (AlphaFold model)
Kinesin heavy chain	W, X, Y	protein	20	DROSOPHILA MELANOGASTER	P17210 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>2Y65_1 KINESIN HEAVY CHAIN (chains A, B, C, D)
MSAEREIPAEDSIKVVCRFRPLNDSEEKAGSKFVVKFPNNVEENCISIAGKVYLFDKVFK
PNASQEKVYNEAAKSIVTDVLAGYNGTIFAYGQTSSGKTHTMEGVIGDSVKQGIIPRIVN
DIFNHIYAMEVNLEFHIKVSYYEIYMDKIRDLLDVSKVNLSVHEDKNRVPYVKGATERFV
SSPEDVFEVIEEGKSNRHIAVTNMNEHSSRSHSVFLINVKQENLENQKKLSGKLYLVDLA
GSEKVSKTGAEGTVLDEAKNINKSLSALGNVISALADGNKTHIPYRDSKLTRILQESLGG
NARTTIVICCSPASFNESETKSTLDFGRRAKTVKNVVCVNEELTAEEWKRRYEKEKEKNA
RLKGK

Sequence of entity 2 (W, X, Y), FASTA

>2Y65_2 KINESIN HEAVY CHAIN (chains W, X, Y)
GSGPQAQIAKPIRSGQGATS

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	4
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	4

Primary citation

The Structure of the Kinesin-1 Motor-Tail Complex Reveals the Mechanism of Autoinhibition. Kaan, H.Y.K., Hackney, D.D., Kozielski, F. Science (2011) 333:883. DOI 10.1126/SCIENCE.1204824 · PubMed

Other PDB entries of the same protein (UniProt P17210 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5JVU 1.95 Å, The neck-linker and alpha 7 helix of Drosophila melanogaster kinesin-1 fused to EB1
5JVR 2.1 Å, The neck-linker of Mus musculus KIF3A fused to the alpha 7 helix of Drosophila…
5JVS 2.25 Å, The neck-linker + DAL and alpha 7 helix of Drosophila melanogaster Kinesin-1 fused to EB1
7BJS 2.28 Å, Crystal structure of Khc/atypical Tm1 complex
2Y5W 2.7 Å, Crystal structure of Drosophila melanogaster kinesin-1 motor domain dimer

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