1TH0: Human Senp2

Structure of human Senp2. Determined by X-ray diffraction at 2.2 Å resolution. Released 14 Sept 2004.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,953
Mol. weight: 53.57 kDa
Released: 14 Sept 2004

Explore 1TH0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1TH0 contains 34 α-helices and 14 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: 17 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	367-369	3
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	413-430	18
α-helix	432-434	3
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	468-475	8	2
β-strand	478-485	8	2
β-strand	490-494	5	2
α-helix	502-519	18
α-helix	526-528	3
β-strand	530-533	4	2
α-helix	534-535	2
α-helix	540-542	3
α-helix	548-559	12
α-helix	569-571	3
α-helix	572-585	14

Chain B: 17 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	370-380	11
β-strand	388-392	5	3
β-strand	395-398	4	3
α-helix	399-402	4
α-helix	403-405	3
α-helix	409-411	3
α-helix	413-429	17
α-helix	432-434	3
β-strand	435-437	3	4
α-helix	442-447	6
α-helix	451-453	3
α-helix	455-458	4
α-helix	463-465	3
β-strand	468-475	8	4
β-strand	478-485	8	4
β-strand	490-494	5	4
α-helix	502-519	18
α-helix	526-528	3
β-strand	530-533	4	4
α-helix	534-535	2
α-helix	540-542	3
α-helix	548-559	12
α-helix	569-571	3
α-helix	572-585	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Sentrin-specific protease 2	A, B	protein	226	Homo sapiens	Q9HC62 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1TH0_1 Sentrin-specific protease 2 (chains A, B)
DLLELTEDMEKEISNALGHGPQDEILSSAFKLRITRGDIQTLKNYHWLNDEVINFYMNLL
VERNKKQGYPALHVFSTFFYPKLKSGGYQAVKRWTKGVNLFEQEIILVPIHRKVHWSLVV
IDLRKKCLKYLDSMGQKGHRICEILLQYLQDESKTKRNSDLNLLEWTHHSMKPHEIPQQL
NGSDCGMFTCKYADYISRDKPITFTQHQMPLFRKKMVWEILHQQLL

Primary citation

A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex. Reverter, D., Lima, C.D. Structure (2004) 12:1519-1531. DOI 10.1016/j.str.2004.05.023 · 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
2IO0 2.3 Å, Crystal structure of human Senp2 in complex with preSUMO-2
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

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