4UBF: HsMCAK motor domain complex

HsMCAK motor domain complex. Determined by X-ray diffraction at 3.0 Å resolution. Released 6 May 2015.

Method: X-ray diffraction
Resolution: 3.0 Å
Organism: Homo sapiens
Chains: 5
Atoms: 9,707
Mol. weight: 176.44 kDa
Ligands: ADP, MG
Released: 6 May 2015

Explore 4UBF in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4UBF contains 57 α-helices and 65 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: 14 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	231-240	10
β-strand	246	1	1
β-strand	262-265	4	2
α-helix	266-268	3
α-helix	270-273	4
α-helix	277-278	2
β-strand	279	1	3
β-strand	281-282	2	4
β-strand	285	1	1
β-strand	289-296	8	4
β-strand	302-309	8	4
β-strand	314-315	2	2
α-helix	321-327	7
α-helix	330-336	7
β-strand	341-348	8	2
α-helix	354-358	5
α-helix	373-383	11
β-strand	396-404	9	2
β-strand	410-411	2	2
β-strand	420-422	3	5
β-strand	430-432	3	5
β-strand	437-439	3	2
α-helix	442-452	11
β-strand	471-479	9	2
β-strand	484-495	12	2
α-helix	516-528	13
α-helix	543-547	5
α-helix	550-552	3
β-strand	562-565	4	2
β-strand	568	1	3
α-helix	569-571	3
α-helix	573-580	8

Chain B: 17 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	231-242	12
α-helix	246-249	4
α-helix	253-255	3
β-strand	259-265	7	6
α-helix	266-269	4
α-helix	270-274	5
α-helix	277-278	2
β-strand	279	1	7
β-strand	282-285	4	4
β-strand	288-293	6	4
β-strand	305-310	6	4
β-strand	313-315	3	6
α-helix	321-325	5
α-helix	330-336	7
β-strand	341-346	6	6
α-helix	373-386	14
β-strand	401-405	5	6
β-strand	408-411	4	6
β-strand	417-418	2	6
β-strand	420-424	5	8
β-strand	430-432	3	8
α-helix	442-455	14
α-helix	467-469	3
β-strand	471-479	9	6
β-strand	484-492	9	6
α-helix	493-495	3
α-helix	515-531	17
α-helix	543-547	5
α-helix	550-552	3
β-strand	557-565	9	6
β-strand	568	1	7
α-helix	571-573	3
α-helix	575-582	8

Chain C: 13 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	231-242	12
α-helix	253	1
β-strand	254-256	3	8
β-strand	259	1	9
β-strand	264-265	2	10
α-helix	266-268	3
α-helix	272-275	4
β-strand	281-282	2	11
β-strand	288-296	9	11
β-strand	302-310	9	11
β-strand	315	1	10
α-helix	321-326	6
α-helix	329-337	9
β-strand	341-346	6	9
β-strand	347-348	2	10
α-helix	354-357	4
α-helix	373-386	14
β-strand	396-405	10	9
β-strand	408-411	4	9
β-strand	417-419	3	9
β-strand	421	1	12
β-strand	431	1	12
β-strand	438-439	2	9
α-helix	442-455	14
β-strand	471-479	9	9
β-strand	484-492	9	9
α-helix	516-531	16
α-helix	543-545	3
α-helix	547-551	5
β-strand	559	1	9
β-strand	563-565	3	10
α-helix	573-579	7

Chain D: 13 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	232-242	11
β-strand	259	1	13
β-strand	264-265	2	13
α-helix	270-274	5
β-strand	281-282	2	11
β-strand	288-296	9	11
β-strand	302-310	9	11
β-strand	315	1	13
α-helix	321-326	6
α-helix	335-338	4
β-strand	342-348	7	13
α-helix	373-381	9
α-helix	388-390	3
α-helix	395	1
β-strand	396-404	9	13
β-strand	409	1	13
α-helix	442-455	14
β-strand	471-479	9	13
β-strand	484-492	9	13
α-helix	516-519	4
α-helix	523-531	9
α-helix	544-547	4
α-helix	550-552	3
β-strand	558-565	8	13
α-helix	572-581	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Kinesin-like protein KIF2C	A, B, C, D	protein	387	Homo sapiens	Q99661 (AlphaFold model)
Kinesin-like protein KIF2C	P	protein	12	Homo sapiens	Q99661 (AlphaFold model)

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

>4UBF_1 Kinesin-like protein KIF2C (chains A, B, C, D)
MGSSHHHHHHSSGLVPRGSSFPNWEFARMIKEFRATLECHPLTMTDPIEEHRICVCVRKR
PLNKQELAKKEIDVISIPSKCLLLVHEPKLKVDLTKYLENQAFCFDFAFDETASNEVVYR
FTARPLVQTIFEGGKATCFAYGQTGSGKTHTMGGDLSGKAQNASKGIYAMASRDVFLLKN
QPCYRKLGLEVYVTFFEIYNGKLFDLLNKKAKLRVLEDGKQQVQVVGLQEHLVNSADDVI
KMIDMGSACRTSGQTFANSNSSRSHACFQIILRAKGRMHGKFSLVDLAGNERGADTSSAD
RQTRMEGAEINKSLLALKECIRALGQNKAHTPFRESKLTQVLRDSFIGENSRTCMIATIS
PGISSCEYTLNTLRYADRVKELSPHSG

Sequence of entity 2 (P), FASTA

>4UBF_2 Kinesin-like protein KIF2C (chains P)
QLEEQASRQISS

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	4
MG	Magnesium ion	Mg	7

Primary citation

The C-terminal region of the motor protein MCAK controls its structure and activity through a conformational switch. Talapatra, S.K., Harker, B., Welburn, J.P. Elife (2015) 4. DOI 10.7554/eLife.06421 · PubMed

Other PDB entries of the same protein (UniProt Q99661 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2HEH 2.15 Å, Crystal Structure of the KIF2C motor domain
4Y05 2.59 Å, KIF2C short Loop2 construct
5MIO 3.19 Å, KIF2C-darpin fusion protein bound to tubulin

Browse structure collections

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