2Y5W: Kinesin heavy chain

Crystal structure of Drosophila melanogaster kinesin-1 motor domain dimer. Determined by X-ray diffraction at 2.7 Å resolution. Released 24 Aug 2011.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: DROSOPHILA MELANOGASTER
Chains: 2
Atoms: 5,388
Mol. weight: 82.67 kDa
Ligands: MG, ADP
Released: 24 Aug 2011

Explore 2Y5W in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2Y5W contains 34 α-helices and 44 β-strands across 2 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: 18 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	12	1	1
α-helix	13	1
β-strand	14-19	6	2
α-helix	21-23	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	65-72	8
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	114-127	14
β-strand	133-144	12	2
β-strand	149-151	3	2
β-strand	160	1	2
β-strand	162-163	2	6
β-strand	171-172	2	6
β-strand	178-180	3	2
α-helix	183-195	13
α-helix	204-210	7
β-strand	212-223	12	2
β-strand	229-238	10	2
α-helix	239-241	3
α-helix	263-276	14
α-helix	285-287	3
α-helix	290-293	4
β-strand	303-310	8	2
β-strand	313	1	3
α-helix	314-316	3
α-helix	317-330	14
α-helix	333	1
β-strand	334	1	1
α-helix	335	1
β-strand	341	1	2
α-helix	345-351	7

Chain B: 16 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	11-12	2	7
β-strand	14-19	6	8
α-helix	20-22	3
α-helix	24-27	4
α-helix	31-32	2
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	76-81	6
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	160	1	8
β-strand	161-164	4	12
β-strand	170-173	4	12
β-strand	178-179	2	8
α-helix	183-196	14
α-helix	204-209	6
β-strand	211-223	13	8
β-strand	229-238	10	8
α-helix	239-241	3
α-helix	263-273	11
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	317-331	15
β-strand	334-335	2	7
β-strand	341-342	2	8
α-helix	345-350	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Kinesin heavy chain	A, B	protein	365	DROSOPHILA MELANOGASTER	P17210 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2Y5W_1 KINESIN HEAVY CHAIN (chains A, B)
MSAEREIPAEDSIKVVCRFRPLNDSEEKAGSKFVVKFPNNVEENCISIAGKVYLFDKVFK
PNASQEKVYNEAAKSIVTDVLAGYNGTIFAYGQTSSGKTHTMEGVIGDSVKQGIIPRIVN
DIFNHIYAMEVNLEFHIKVSYYEIYMDKIRDLLDVSKVNLSVHEDKNRVPYVKGATERFV
SSPEDVFEVIEEGKSNRHIAVTNMNEHSSRSHSVFLINVKQENLENQKKLSGKLYLVDLA
GSEKVSKTGAEGTVLDEAKNINKSLSALGNVISALADGNKTHIPYRDSKLTRILQESLGG
NARTTIVICCSPASFNESETKSTLDFGRRAKTVKNVVCVNEELTAEEWKRRYEKEKEKNA
RLKGK

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	2
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	2

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…
2Y65 2.2 Å, Crystal structure of Drosophila melanogaster kinesin-1 motor domain dimer-tail complex
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

Browse structure collections

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