5LSJ: Protein MIS12 homolog

Crystal structure of the human kinetochore MIS12-cenp-C delta-HEAD2 complex. Determined by X-ray diffraction at 3.25 Å resolution. Released 16 Nov 2016.

Method: X-ray diffraction
Resolution: 3.25 Å
Organism: Homo sapiens
Chains: 10
Atoms: 9,621
Mol. weight: 173.56 kDa
Released: 16 Nov 2016

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

Secondary structure: helices and β-sheets

5LSJ contains 38 α-helices and 0 β-strands across 8 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: 6 helices, 0 β-strands

Element	Residues	Length
α-helix	17-47	31
α-helix	57-89	33
α-helix	100-102	3
α-helix	104-106	3
α-helix	111-167	57
α-helix	174-197	24

Chain B: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	35-51	17
α-helix	56-61	6
α-helix	63-66	4
α-helix	70-96	27
α-helix	101-115	15
α-helix	121-123	3
α-helix	129-188	60
α-helix	190-200	11

Chain C: 6 helices, 0 β-strands

Element	Residues	Length
α-helix	17-48	32
α-helix	58-89	32
α-helix	100-102	3
α-helix	108-110	3
α-helix	111-167	57
α-helix	174-198	25

Chains D and F: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	204-242	39
α-helix	265-269	5
α-helix	274-314	41

Chain E: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	35-51	17
α-helix	55-59	5
α-helix	63-66	4
α-helix	70-96	27
α-helix	101-115	15
α-helix	121-123	3
α-helix	129-188	60
α-helix	190-200	11

Chain G: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	105-149	45
α-helix	170-200	31

Chain N: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	106-149	44
α-helix	170-200	31

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein MIS12 homolog	A, C	protein	205	Homo sapiens	Q9H081 (AlphaFold model)
Polyamine-modulated factor 1	B, E	protein	176	Homo sapiens	Q6P1K2 (AlphaFold model)
Kinetochore-associated protein DSN1 homolog	D, F	protein	178	Homo sapiens	Q9H410 (AlphaFold model)
Kinetochore-associated protein NSL1 homolog	G, N	protein	116	Homo sapiens	Q96IY1 (AlphaFold model)
Centromere protein C	P, Q	protein	76	Homo sapiens	Q03188

Sequence of entity 1 (A, C), FASTA

>5LSJ_1 Protein MIS12 homolog (chains A, C)
MSVDPMTYEAQFFGFTPQTCMLRIYIAFQDYLFEVMQAVEQVILKKLDGIPDCDISPVQI
RKCTEKFLCFMKGHFDNLFSKMEQLFLQLILRIPSNILLPEDKCKETPYSEEDFQHLQKE
IEQLQEKYKTELCTKQALLAELEEQKIVQAKLKQTLTFFDELHNVGRDHGTSDFRESLVS
LVQNSRKLQNIRDNVEKESKRLKIS

Sequence of entity 2 (B, E), FASTA

>5LSJ_2 Polyamine-modulated factor 1 (chains B, E)
MTISRVKLLDTMVDTFLQKLVAAGSYQRFTDCYKCFYQLQPAMTQQIYDKFIAQLQTSIR
EEISDIKEEGNLEAVLNALDKIVEEGKVRKEPAWRPSGIPEKDLHSVMAPYFLQQRDTLR
RHVQKQEAENQQLADAVLAGRRQVEELQLQVQAQQQAWQALHREQRELVAVLREPE

Sequence of entity 3 (D, F), FASTA

>5LSJ_3 Kinetochore-associated protein DSN1 homolog (chains D, F)
MGTLQKCFEDSNGKASDFSLEASVAEMKEYITKFSLERQTWDQLLLHYQQEAKEILSRGS
TEAKITEVKVEPMTYLGSSQNEVLNTKPDYQKILQNQSKVFDCMELVMDELQGSVKQLQA
FMDESTQCFQKVSVQLGKRSMQQLDPSPARKLLKLQLQNPPAIHGSGSGSCQHHHHHH

Sequence of entity 4 (G, N), FASTA

>5LSJ_4 Kinetochore-associated protein NSL1 homolog (chains G, N)
MGQAWQEASDNCFMDSDIKVLEDQFDEIIVDIATKRKQYPRKILECVIKTIKAKQEILKQ
YHPVVHPLDLKYDPDPAPHMENLKCRGETVAKEISEAMKSLPALIEQGEGFSQVLR

Sequence of entity 5 (P, Q), FASTA

>5LSJ_5 Centromere protein C (chains P, Q)
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
5LSK 3.5 Å, Crystal structure of the human kinetochore MIS12-cenp-C complex
8Q5H 4.5 Å, Human KMN network (outer kinetochore)

Browse structure collections

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