4OUC: Human haspin

Structure of human haspin in complex with histone H3 substrate. Determined by X-ray diffraction at 1.9 Å resolution. Released 16 Apr 2014.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,214
Mol. weight: 43.04 kDa
Ligands: 5ID
Released: 16 Apr 2014

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

Secondary structure: helices and β-sheets

4OUC contains 17 α-helices and 19 β-strands across 1 chain. 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: 17 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	473-474	2	1
α-helix	475-478	4
α-helix	481-485	5
β-strand	488-493	6	1
β-strand	496-503	8	1
β-strand	506-515	10	1
β-strand	521	1	2
β-strand	524	1	2
α-helix	525-526	2
β-strand	527	1	1
α-helix	528	1
α-helix	529-544	16
β-strand	552	1	3
β-strand	559-566	8	1
α-helix	569-570	2
α-helix	571-583	13
α-helix	589-590	2
β-strand	599-606	8	1
β-strand	610-611	2	4
α-helix	622-643	22
β-strand	646	1	5
α-helix	652-654	3
β-strand	655-659	5	4
β-strand	664-669	6	3
β-strand	672-677	6	3
β-strand	681-685	5	4
β-strand	692	1	5
β-strand	693-695	3	6
β-strand	698-700	3	6
α-helix	708-711	4
α-helix	717-729	13
α-helix	739-754	16
α-helix	765-780	16
α-helix	781-783	3
α-helix	787-793	7
α-helix	795-797	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine-protein kinase haspin	A	protein	357	Homo sapiens	Q8TF76 (AlphaFold model)
Histone H3.2	B	protein	12	Homo sapiens	Q71DI3 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4OUC_1 Serine/threonine-protein kinase haspin (chains A)
MHHHHHHSSGVDLGTENLYFQSMGECSQKGPVPFSHCLPTEKLQRCEKIGEGVFGEVFQT
IADHTPVAIKIIAIEGPDLVNGSHQKTFEEILPEIIISKELSLLSGEVCNRTEGFIGLNS
VHCVQGSYPPLLLKAWDHYNSTKGSANDRPDFFKDDQLFIVLEFEFGGIDLEQMRTKLSS
LATAKSILHQLTASLAVAEASLRFEHRDLHWGNVLLKKTSLKKLHYTLNGKSSTIPSCGL
QVSIIDYTLSRLERDGIVVFCDVSMDEDLFTGDGDYQFDIYRLMKKENNNRWGEYHPYSN
VLWLHYLTDKMLKQMTFKTKCNTPAMKQIKRKIQEFHRTMLNFSSATDLLCQHSLFK

Sequence of entity 2 (B), FASTA

>4OUC_2 Histone H3.2 (chains B)
ARTKQTARKSTY

Ligands and cofactors

ID	Name	Formula	Copies
5ID	(2R,3R,4S,5R)-2-(4-amino-5-iodo-7H-PYRROLO[2,3-d]pyrimidin-7-yl)-5-(hydroxymeth…	C11 H13 I N4 O4	1

Water and common crystallization additives (NA, EDO, IOD) are not listed.

Primary citation

Modulation of the chromatin phosphoproteome by the haspin protein kinase. Maiolica, A., de Medina-Redondo, M., Schoof, E.M. et al. Mol Cell Proteomics (2014) 13:1724-1740. DOI 10.1074/mcp.M113.034819 · PubMed

Other PDB entries of the same protein (UniProt Q8TF76 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4QTC 1.4 Å, Structure of human haspin (GSG2) in complex with SCH772984 revealing the first type-I…
6G3A 1.43 Å, Crystal structure of haspin F605T mutant in complex with 5-iodotubercidin
6G39 1.45 Å, Crystal structure of haspin F605Y mutant in complex with 5-iodotubercidin
6G36 1.46 Å, Crystal structure of haspin in complex with 5-chlorotubercidin
6G38 1.47 Å, Crystal structure of haspin in complex with tubercidin
6G37 1.48 Å, Crystal structure of haspin in complex with 5-fluorotubercidin
5HTC 1.5 Å, Crystal structure of haspin (GSG2) in complex with bisubstrate inhibitor ARC-3372
6Z57 1.5 Å, Crystal structure of haspin (GSG2) in complex with macrocycle ODS2004078
6Z5E 1.5 Å, Crystal structure of haspin (GSG2) in complex with macrocycle ODS2004093
6G35 1.55 Å, Crystal structure of haspin in complex with 5-bromotubercidin
6Z5A 1.55 Å, Crystal structure of haspin (GSG2) in complex with macrocycle ODS2002941
7AVQ 1.65 Å, Crystal structure of haspin in complex with disubstituted imidazo[1,2- b]pyridazine…

Browse structure collections

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