9ESA: Aurora-C with SER mutation

Aurora-C with SER mutation in complex with INCENP peptide. Determined by X-ray diffraction at 2.8 Å resolution. Released 11 Sept 2024.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 4
Atoms: 5,297
Mol. weight: 83.75 kDa
Released: 11 Sept 2024

Explore 9ESA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9ESA contains 41 α-helices and 18 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 AAA: 16 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	40-42	3
β-strand	43-51	9	1
β-strand	56-62	7	1
β-strand	68-75	8	1
α-helix	76-81	6
α-helix	85-97	13
β-strand	103	1	2
β-strand	106-111	6	1
β-strand	115-120	6	1
β-strand	127	1	2
α-helix	128-135	8
α-helix	140-159	20
α-helix	169-171	3
β-strand	172-174	3	2
β-strand	180-182	3	2
α-helix	194-200	7
α-helix	203-205	3
α-helix	208-211	4
α-helix	220-234	15
α-helix	244-252	9
α-helix	264-273	10
α-helix	278-280	3
α-helix	284-288	5
α-helix	291-296	6
α-helix	301-303	3

Chain BBB: 17 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	40-42	3
β-strand	43-51	9	3
β-strand	56-62	7	3
β-strand	68-75	8	3
α-helix	76-81	6
α-helix	85-97	13
β-strand	103	1	4
β-strand	106-111	6	3
β-strand	115-120	6	3
β-strand	127	1	4
α-helix	128-135	8
α-helix	140-159	20
α-helix	165-167	3
α-helix	169-171	3
β-strand	172-174	3	4
β-strand	180-182	3	4
α-helix	194-200	7
α-helix	203-205	3
α-helix	208-211	4
α-helix	220-234	15
α-helix	244-252	9
α-helix	264-273	10
α-helix	278-280	3
α-helix	284-288	5
α-helix	291-296	6
α-helix	301-303	3

Chains CCC and DDD: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	844-846	3
α-helix	848-860	13
α-helix	865-869	5
α-helix	877-880	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Aurora kinase C	AAA, BBB	protein	303	Homo sapiens	Q9UQB9 (AlphaFold model)
Inner centromere protein	CCC, DDD	protein	58	Homo sapiens	Q9NQS7 (AlphaFold model)

Sequence of entity 1 (AAA, BBB), FASTA

>9ESA_1 Aurora kinase C (chains AAA, BBB)
HHHHHHAQPAGEELATANQTAQQPSSPAMRRLTVDDFEIGRPLGKGKFGNVYLARLKESH
FIVALKVLFKSQIEKEGLEHQLRREIEIQAHLQHPNILRLYNYFHDARRVYLILEYAPRG
ELYKELQKSEKLDEQRTATIIEELADALTYCHDKKVIHRDIKPENLLLGFRGEVKIADFG
WSVHTPSLAAATMCGTLDYLPPEMIEGRTYDEKVDLWCIGVLCYELLVGYPPFESASHSE
TYRRILKVDVRFPLSMPLGARDLISRLLRYQPLERLPLAQILKHPWVQAHSRRVLPPCAQ
MAS

Sequence of entity 2 (CCC, DDD), FASTA

>9ESA_2 Inner centromere protein (chains CCC, DDD)
DEAHPRKPIPTWARGTPLSQAIIHQYYHPPNLLELFGTILPLDLEDIFKKSKPRYHKR

Primary citation

Surface-mutagenesis strategies to enable structural biology crystallization platforms. Schaefer, M., Putter, V., Hilpmann, A. et al. Acta Crystallogr D Struct Biol (2024) 80:661-674. DOI 10.1107/S2059798324007939 · PubMed

Other PDB entries of the same protein (UniProt Q9UQB9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6GR8 1.75 Å, Human AURKC INCENP complex bound to BRD-7880
6GR9 2.25 Å, Human AURKC INCENP complex bound to VX-680

Browse structure collections

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