5LSK: Human kinetochore MIS12-cenp-C complex

Crystal structure of the human kinetochore MIS12-cenp-C complex. Determined by X-ray diffraction at 3.5 Å resolution. Released 16 Nov 2016.

Method: X-ray diffraction
Resolution: 3.5 Å
Organism: Homo sapiens
Chains: 5
Atoms: 6,192
Mol. weight: 110.35 kDa
Released: 16 Nov 2016

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

Secondary structure: helices and β-sheets

5LSK contains 29 α-helices and 2 β-strands across 5 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: 7 helices, 0 β-strands

Element	Residues	Length
α-helix	9-13	5
α-helix	17-45	29
α-helix	58-89	32
α-helix	100-102	3
α-helix	104-106	3
α-helix	111-167	57
α-helix	178-196	19

Chain B: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	34-52	19
α-helix	55-60	6
α-helix	63-66	4
α-helix	72-96	25
α-helix	101-115	15
α-helix	121-122	2
α-helix	129-188	60
α-helix	190-200	11

Chain D: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	117-120	4
α-helix	131-149	19
α-helix	162-185	24
α-helix	189-192	4
α-helix	204-240	37
α-helix	265-269	5
α-helix	274-312	39
α-helix	313-316	4

Chain N: 5 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	38-39	2	1
α-helix	43-59	17
α-helix	60-62	3
α-helix	69-86	18
β-strand	88-89	2	1
α-helix	105-149	45
α-helix	170-200	31

Chain P: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	35-41	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein MIS12 homolog	A	protein	205	Homo sapiens	Q9H081 (AlphaFold model)
Polyamine-modulated factor 1	B	protein	176	Homo sapiens	Q6P1K2 (AlphaFold model)
Kinetochore-associated protein DSN1 homolog	D	protein	296	Homo sapiens	Q9H410 (AlphaFold model)
Kinetochore-associated protein NSL1 homolog	N	protein	206	Homo sapiens	Q96IY1 (AlphaFold model)
Centromere protein C	P	protein	76	Homo sapiens	Q03188

Sequence of entity 1 (A), FASTA

>5LSK_1 Protein MIS12 homolog (chains A)
MSVDPMTYEAQFFGFTPQTCMLRIYIAFQDYLFEVMQAVEQVILKKLDGIPDCDISPVQI
RKCTEKFLCFMKGHFDNLFSKMEQLFLQLILRIPSNILLPEDKCKETPYSEEDFQHLQKE
IEQLQEKYKTELCTKQALLAELEEQKIVQAKLKQTLTFFDELHNVGRDHGTSDFRESLVS
LVQNSRKLQNIRDNVEKESKRLKIS

Sequence of entity 2 (B), FASTA

>5LSK_2 Polyamine-modulated factor 1 (chains B)
MTISRVKLLDTMVDTFLQKLVAAGSYQRFTDCYKCFYQLQPAMTQQIYDKFIAQLQTSIR
EEISDIKEEGNLEAVLNALDKIVEEGKVRKEPAWRPSGIPEKDLHSVMAPYFLQQRDTLR
RHVQKQEAENQQLADAVLAGRRQVEELQLQVQAQQQAWQALHREQRELVAVLREPE

Sequence of entity 3 (D), FASTA

>5LSK_3 Kinetochore-associated protein DSN1 homolog (chains D)
MSHQERLQSKSLHLSPQEQSASYQDRRQSWRRASMKETNRRKSLHPIHQGITELSRSISV
DLAESKRLGCLLLSSFQFSIQKLEPFLRDTKGFSLESFRAKASSLSEELKHFADGLETDG
TLQKCFEDSNGKASDFSLEASVAEMKEYITKFSLERQTWDQLLLHYQQEAKEILSRGSTE
AKITEVKVEPMTYLGSSQNEVLNTKPDYQKILQNQSKVFDCMELVMDELQGSVKQLQAFM
DESTQCFQKVSVQLGKRSMQQLDPSPARKLLKLQLQNPPAIHGSGSGSCQHHHHHH

Sequence of entity 4 (N), FASTA

>5LSK_4 Kinetochore-associated protein NSL1 homolog (chains N)
MAGSPELVVLDPPWDKELAAGTESQALVSATPREDFRVRCTSKRAVTEMLQLCGRFVQKL
GDALPEEIREPALRDAQWTFESAVQENISINGQAWQEASDNCFMDSDIKVLEDQFDEIIV
DIATKRKQYPRKILECVIKTIKAKQEILKQYHPVVHPLDLKYDPDPAPHMENLKCRGETV
AKEISEAMKSLPALIEQGEGFSQVLR

Sequence of entity 5 (P), FASTA

>5LSK_5 Centromere protein C (chains P)
GPLGSMAASGLDHLKNGYRRRFCRPSRARDINTEQGQNVLEILQDCFEEKSLANDFSTNS
TKSVPNSTRKIKDTCI

Primary citation

Structure of the MIS12 Complex and Molecular Basis of Its Interaction with CENP-C at Human Kinetochores. Petrovic, A., Keller, J., Liu, Y. et al. Cell (2016) 167:1028-1040.e15. DOI 10.1016/j.cell.2016.10.005 · PubMed

Other PDB entries of the same protein (UniProt Q9H081 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8PPR 3.0 Å, Structure of the human outer kinetochore KMN network complex
5LSJ 3.25 Å, Crystal structure of the human kinetochore MIS12-cenp-C delta-HEAD2 complex
8Q5H 4.5 Å, Human KMN network (outer kinetochore)

Browse structure collections

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