3KIN: Kinesin (dimeric) from rattus norvegicus

Kinesin (dimeric) from rattus norvegicus. Determined by X-ray diffraction at 3.1 Å resolution. Released 14 Oct 1998.

Method: X-ray diffraction
Resolution: 3.1 Å
Organism: Rattus norvegicus
Chains: 4
Atoms: 5,743
Mol. weight: 81.5 kDa
Ligands: ADP
Released: 14 Oct 1998

Explore 3KIN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3KIN contains 36 α-helices and 43 β-strands across 4 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: 9 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	5-8	4	1
α-helix	9	1
β-strand	10-15	6	2
α-helix	16-19	4
α-helix	20-24	5
β-strand	31-34	4	3
β-strand	38-41	4	3
β-strand	47-48	2	3
β-strand	51-53	3	2
α-helix	59-66	8
α-helix	68-75	8
β-strand	80-85	6	2
α-helix	92-96	5
β-strand	98	1	4
β-strand	106	1	4
α-helix	108-122	15
β-strand	127-139	13	2
β-strand	142-145	4	2
β-strand	154	1	2
β-strand	156-158	3	5
β-strand	164-166	3	5
β-strand	172-174	3	2
α-helix	177-190	14
α-helix	198-202	5
β-strand	205-217	13	2
β-strand	223-232	10	2

Chain B: 8 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	258-271	14
α-helix	279-281	3
α-helix	283-287	5
α-helix	289-293	5
β-strand	297-304	8	2
α-helix	308-310	3
α-helix	311-324	14
β-strand	328-331	4	1
β-strand	335	1	2
α-helix	339-366	28
α-helix	367-371	5

Chain C: 9 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	5-8	4	6
α-helix	9	1
β-strand	10-15	6	7
α-helix	16-17	2
α-helix	20-25	6
β-strand	29	1	8
β-strand	31-34	4	9
β-strand	38-41	4	9
β-strand	47-48	2	9
β-strand	51-53	3	7
α-helix	59-66	8
α-helix	68-76	9
β-strand	80-85	6	7
α-helix	92-96	5
β-strand	98	1	10
β-strand	106	1	10
α-helix	108-122	15
β-strand	127-128	2	7
β-strand	131-139	9	7
β-strand	142-145	4	7
β-strand	154	1	7
β-strand	156-158	3	11
β-strand	164-166	3	11
β-strand	172-174	3	7
α-helix	177-190	14
α-helix	198-203	6
β-strand	206-217	12	7
β-strand	223-232	10	7

Chain D: 10 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	257-271	15
α-helix	279-281	3
α-helix	283-287	5
α-helix	289-293	5
β-strand	297-304	8	7
β-strand	307	1	8
α-helix	308-310	3
α-helix	311-324	14
β-strand	328-331	4	6
β-strand	334-336	3	7
α-helix	337-338	2
α-helix	339-361	23
α-helix	362-364	3
α-helix	366-369	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Kinesin heavy chain	A, C	protein	238	Rattus norvegicus	P56536 (AlphaFold model)
Kinesin heavy chain	B, D	protein	117	Rattus norvegicus	Q6QLM7 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>3KIN_1 KINESIN HEAVY CHAIN (chains A, C)
ADPAECSIKVMCRFRPLNEAEILRGDKFIPKFKGEETVVIGQGKPYVFDRVLPPNTTQEQ
VYNACAKQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIAHDIFDHIY
SMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNRVPYVKGCTERFVSSPEEVM
DVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSGKLYLVDLAGSEKV

Sequence of entity 2 (B, D), FASTA

>3KIN_2 KINESIN HEAVY CHAIN (chains B, D)
NKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETK
STLMFGQRAKTIKNTVSVNLELTAEEWKKKYEKEKEKNKALKSVIQHLEVELNRWRN

Ligands and cofactors

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

Primary citation

The crystal structure of dimeric kinesin and implications for microtubule-dependent motility. Kozielski, F., Sack, S., Marx, A. et al. Cell (1997) 91:985-994. DOI 10.1016/S0092-8674(00)80489-4 · PubMed

Other PDB entries of the same protein (UniProt P56536 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2KIN 2.0 Å, Kinesin (monomeric) from rattus norvegicus
5HLE 2.9 Å, Structural basis of backwards motion in kinesin-14: minus-end directed nKn664 in the ADP…
5HNZ 5.8 Å, Structural basis of backwards motion in kinesin-14: plus-end directed nKn669 in the…
5HNY 6.3 Å, Structural basis of backwards motion in kinesin-14: plus-end directed nKn669 in the…
5HNW 6.6 Å, Structural basis of backwards motion in kinesin-14: minus-end directed nKn664 in the…
5HNX 6.6 Å, Structural basis of backwards motion in kinesin-14: minus-end directed nKn664 in the…
8TT7 NMR Assignments and Structure for the Dimeric Kinesin Neck Domain

Browse more

3KIN is part of these collections:

Motor proteins and the cytoskeleton

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