5LT4: Kinesin-1 heavy chain

nucleotide-free kinesin-1 motor domain T92V mutant, P1 crystal form. Determined by X-ray diffraction at 2.88 Å resolution. Released 1 Mar 2017.

Method: X-ray diffraction
Resolution: 2.88 Å
Organism: Homo sapiens
Chains: 6
Atoms: 14,147
Mol. weight: 218.8 kDa
Released: 1 Mar 2017

Explore 5LT4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5LT4 contains 82 α-helices and 116 β-strands across 6 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: 14 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	9-15	7	1
α-helix	16-17	2
β-strand	32-34	3	2
β-strand	38-41	4	2
β-strand	44-47	4	2
β-strand	50-52	3	1
α-helix	58-61	4
α-helix	62-66	5
α-helix	67-73	7
β-strand	79-85	7	1
α-helix	91-95	5
β-strand	97	1	3
β-strand	99	1	4
β-strand	101	1	4
β-strand	105	1	3
α-helix	107-120	14
β-strand	126-138	13	1
β-strand	141-144	4	1
β-strand	153	1	1
β-strand	154-157	4	5
β-strand	163-166	4	5
β-strand	171-173	3	1
α-helix	176-187	12
β-strand	192-193	2	6
β-strand	201-202	2	6
β-strand	205-216	12	1
β-strand	222-231	10	1
α-helix	232-235	4
α-helix	246-269	24
α-helix	277-279	3
α-helix	281-285	5
α-helix	287-289	3
β-strand	295-302	8	1
α-helix	306-308	3
α-helix	309-320	12

Chain B: 16 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-15	8	7
α-helix	16-19	4
α-helix	20-23	4
β-strand	29	1	8
β-strand	32-34	3	9
β-strand	38-41	4	9
β-strand	44-47	4	9
β-strand	50-52	3	7
α-helix	58-62	5
α-helix	63-67	5
α-helix	68-73	6
β-strand	79-85	7	7
α-helix	91-95	5
β-strand	97	1	10
β-strand	105	1	10
α-helix	107-122	16
β-strand	126-138	13	7
β-strand	141-144	4	7
β-strand	153	1	7
β-strand	155-157	3	11
β-strand	163-165	3	11
β-strand	171-173	3	7
α-helix	176-187	12
β-strand	205-216	12	7
β-strand	221-232	12	7
α-helix	233-235	3
α-helix	248-269	22
α-helix	277-279	3
α-helix	281-285	5
α-helix	287-289	3
β-strand	295-302	8	7
β-strand	305	1	8
α-helix	306-308	3
α-helix	309-319	11
α-helix	320-322	3

Chain C: 13 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	9-15	7	12
α-helix	16-17	2
β-strand	32-33	2	13
β-strand	38-41	4	13
β-strand	44-47	4	13
β-strand	50-52	3	12
α-helix	58-65	8
α-helix	67-73	7
β-strand	79-85	7	12
α-helix	91-95	5
β-strand	97	1	14
β-strand	105	1	14
α-helix	107-120	14
β-strand	126-138	13	12
β-strand	141-144	4	12
β-strand	153	1	12
β-strand	154-157	4	15
β-strand	163-166	4	15
β-strand	171-173	3	12
α-helix	176-187	12
β-strand	205-216	12	12
β-strand	221-233	13	12
α-helix	234-235	2
α-helix	246-269	24
α-helix	277-279	3
α-helix	281-285	5
α-helix	287-289	3
β-strand	295-302	8	12
α-helix	306-308	3
α-helix	309-320	12

Chain D: 13 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	9-15	7	16
α-helix	22-24	3
β-strand	31-34	4	17
β-strand	38-41	4	17
β-strand	44-47	4	17
β-strand	50-52	3	16
α-helix	58-65	8
α-helix	67-73	7
β-strand	79-85	7	16
α-helix	91-95	5
β-strand	97	1	18
β-strand	105	1	18
α-helix	107-120	14
β-strand	126-138	13	16
β-strand	141-144	4	16
β-strand	153	1	16
β-strand	154-157	4	19
β-strand	163-166	4	19
β-strand	171-173	3	16
α-helix	176-187	12
β-strand	192-194	3	20
β-strand	200-202	3	20
β-strand	205-216	12	16
β-strand	222-231	10	16
α-helix	232-235	4
α-helix	246-269	24
α-helix	277-279	3
α-helix	281-285	5
α-helix	287-289	3
β-strand	295-302	8	16
α-helix	306-308	3
α-helix	309-320	12

Chain E: 13 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	9-15	7	21
α-helix	16-18	3
β-strand	29	1	22
β-strand	32-34	3	23
β-strand	38-41	4	23
β-strand	44-47	4	23
β-strand	50-52	3	21
α-helix	58-65	8
α-helix	67-73	7
β-strand	79-84	6	21
α-helix	91-95	5
β-strand	97	1	24
β-strand	105	1	24
α-helix	107-120	14
β-strand	126-138	13	21
β-strand	141-144	4	21
β-strand	153	1	21
β-strand	154-157	4	25
β-strand	163-166	4	25
α-helix	168-170	3
β-strand	171-173	3	21
α-helix	176-187	12
β-strand	192-193	2	26
β-strand	201-202	2	26
β-strand	205-216	12	21
β-strand	222-232	11	21
α-helix	233-235	3
α-helix	245-269	25
α-helix	277-279	3
α-helix	281-285	5
α-helix	287-289	3
β-strand	295-302	8	21
β-strand	305	1	22
α-helix	309-320	12

Chain K: 13 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	9-15	7	27
α-helix	16-17	2
α-helix	23-25	3
β-strand	32-34	3	28
β-strand	38-41	4	28
β-strand	44-47	4	28
β-strand	50-52	3	27
α-helix	58-65	8
α-helix	67-73	7
β-strand	79-85	7	27
α-helix	91-95	5
β-strand	97	1	29
β-strand	105	1	29
α-helix	107-122	16
β-strand	126-138	13	27
β-strand	141-144	4	27
β-strand	153	1	27
β-strand	154-157	4	30
β-strand	163-166	4	30
β-strand	171-173	3	27
α-helix	176-187	12
β-strand	192	1	31
β-strand	202	1	31
β-strand	205-216	12	27
β-strand	222-233	12	27
α-helix	234-235	2
α-helix	246-269	24
α-helix	277-279	3
α-helix	281-285	5
α-helix	287-289	3
β-strand	295-302	8	27
α-helix	309-320	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Kinesin-1 heavy chain	A, B, C, D, E, K	protein	325	Homo sapiens	P33176 (AlphaFold model)

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

>5LT4_1 Kinesin-1 heavy chain (chains A, B, C, D, E, K)
MADLAESNIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVIASKPYAFDRVFQSSTSQEQ
VYNDAAKKIVKDVLEGYNGTIFAYGQTSSGKVHTMEGKLHDPEGMGIIPRIVQDIFNYIY
SMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNRVPYVKGATERFVSSPDEVM
DTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSK
TGAEGAVLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSLGGNARTTIVI
CCSPSSYNESETKSTLLFGQRAKTI

Primary citation

The structural switch of nucleotide-free kinesin. Cao, L., Cantos-Fernandes, S., Gigant, B. Sci Rep (2017) 7:42558-42558. DOI 10.1038/srep42558 · PubMed

Other PDB entries of the same protein (UniProt P33176 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1BG2 1.8 Å, Human ubiquitous kinesin motor domain
5LT1 1.95 Å, nucleotide-free kinesin-1 motor domain T92V mutant, P21 crystal form
5LT0 2.0 Å, nucleotide-free kinesin-1 motor domain, P212121 crystal form
4LNU 2.19 Å, Nucleotide-free kinesin motor domain in complex with tubulin and a DARPin
9L7E 2.4 Å, Crystal structure of human kinesin-1 motor domain (G234A mutant) in complex with ADP
5LT3 2.59 Å, nucleotide-free kinesin-1 motor domain T87A mutant, P1 crystal form
5LT2 2.6 Å, nucleotide-free kinesin-1 motor domain, P1 crystal form
1MKJ 2.7 Å, Human Kinesin Motor Domain With Docked Neck Linker
9L6K 2.8 Å, Crystal structure of nucleotide-free human kinesin-1 motor domain (G234V mutant)
9L78 2.82 Å, Crystal structure of nucleotide-free human kinesin-1 motor domain (G234A mutant)
9GNQ 2.9 Å, Microtubule-associated Kif5B IAK tail mutant bound to ADP
7TR2 3.0 Å, Apo CaKip3[2-436]-L2-mutant(HsKHC) in complex with a microtubule

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