2IO0: Human Senp2

Crystal structure of human Senp2 in complex with preSUMO-2. Determined by X-ray diffraction at 2.3 Å resolution. Released 14 Nov 2006.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,709
Mol. weight: 38.23 kDa
Released: 14 Nov 2006

Explore 2IO0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2IO0 contains 17 α-helices and 13 β-strands across 2 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: 16 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	370-380	11
β-strand	388-392	5	1
β-strand	395-398	4	1
α-helix	399-402	4
α-helix	403-405	3
α-helix	409-411	3
α-helix	413-429	17
β-strand	435-437	3	2
α-helix	442-449	8
α-helix	451-453	3
α-helix	455-458	4
α-helix	463-465	3
β-strand	468-474	7	2
β-strand	479-485	7	2
β-strand	490-494	5	2
α-helix	503-515	13
α-helix	516-520	5
β-strand	530	1	2
β-strand	533	1	2
α-helix	536-538	3
α-helix	545-547	3
α-helix	548-561	14
α-helix	569-571	3
α-helix	572-585	14

Chain B: 1 helix, 5 β-strands

Element	Residues	Length	Sheet
β-strand	17-23	7	3
β-strand	29-35	7	3
α-helix	41-50	10
β-strand	58-62	5	3
β-strand	65-66	2	3
β-strand	82-88	7	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Sentrin-specific protease 2	A	protein	232	Homo sapiens	Q9HC62 (AlphaFold model)
Small ubiquitin-related modifier 2 precursor	B	protein	91	Homo sapiens	P61956 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2IO0_1 Sentrin-specific protease 2 (chains A)
GSHMASDLLELTEDMEKEISNALGHGPQDEILSSAFKLRITRGDIQTLKNYHWLNDEVIN
FYMNLLVERNKKQGYPALHVFSTFFYPKLKSGGYQAVKRWTKGVNLFEQEIILVPIHRKV
HWSLVVIDLRKKCLKYLDSMGQKGHRICEILLQYLQDESKTKRNSDLNLLEWTHHSMKPH
EIPQQLNGSDSGMFTCKYADYISRDKPITFTQHQMPLFRKKMVWEILHQQLL

Sequence of entity 2 (B), FASTA

>2IO0_2 Small ubiquitin-related modifier 2 precursor (chains B)
MANDHINLKVAGQDGSVVQFKIKRHTPLSKLMKAYCERQGLSMRQIRFRFDGQPINETDT
PAQLEMEDEDTIDVFQQQTGGVYLEHHHHHH

Primary citation

Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Reverter, D., Lima, C.D. Nat Struct Mol Biol (2006) 13:1060-1068. DOI 10.1038/nsmb1168 · PubMed

Other PDB entries of the same protein (UniProt Q9HC62 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3ZO5 2.15 Å, Structure of SENP2-Loop1 in complex with preSUMO-2
1TH0 2.2 Å, Structure of human Senp2
2IO1 2.6 Å, Crystal structure of human Senp2 in complex with preSUMO-3
1TGZ 2.8 Å, Structure of human Senp2 in complex with SUMO-1
2IO2 2.9 Å, Crystal structure of human Senp2 in complex with RanGAP1-SUMO-1
5AEK 3.0 Å, Crystal structure of the human SENP2 C548S in complex with the human SUMO1 K48M F66W
2IO3 3.2 Å, Crystal structure of human Senp2 in complex with RanGAP1-SUMO-2

Browse structure collections

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