2IO1: Human Senp2
Crystal structure of human Senp2 in complex with preSUMO-3. Determined by X-ray diffraction at 2.6 Å resolution. Released 14 Nov 2006.
- Method
- X-ray diffraction
- Resolution
- 2.6 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 7,816
- Mol. weight
- 113.8 kDa
- Released
- 14 Nov 2006
Explore 2IO1 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2IO1 contains 50 α-helices and 42 β-strands across 6 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: 13 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 | 409-410 | 2 | |
| β-strand | 411-412 | 2 | 2 |
| α-helix | 413-430 | 18 | |
| β-strand | 435-437 | 3 | 3 |
| α-helix | 442-454 | 13 | |
| α-helix | 455-458 | 4 | |
| α-helix | 463-465 | 3 | |
| β-strand | 468-475 | 8 | 3 |
| β-strand | 478-485 | 8 | 3 |
| α-helix | 486-488 | 3 | |
| β-strand | 490-494 | 5 | 3 |
| α-helix | 502-520 | 19 | |
| β-strand | 530-533 | 4 | 3 |
| α-helix | 534-535 | 2 | |
| α-helix | 548-560 | 13 | |
| α-helix | 572-585 | 14 | |
Chain B: 2 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 16-22 | 7 | 4 |
| β-strand | 28-34 | 7 | 4 |
| α-helix | 40-50 | 11 | |
| α-helix | 54-56 | 3 | |
| β-strand | 57-61 | 5 | 4 |
| β-strand | 64-65 | 2 | 4 |
| β-strand | 82-87 | 6 | 4 |
| β-strand | 90-91 | 2 | 2 |
Chain C: 15 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 370-380 | 11 | |
| β-strand | 388-392 | 5 | 5 |
| β-strand | 395-398 | 4 | 5 |
| α-helix | 399-402 | 4 | |
| α-helix | 403-405 | 3 | |
| β-strand | 412 | 1 | 6 |
| α-helix | 413-430 | 18 | |
| α-helix | 432-434 | 3 | |
| β-strand | 435-437 | 3 | 7 |
| α-helix | 442-449 | 8 | |
| α-helix | 451-454 | 4 | |
| α-helix | 455-458 | 4 | |
| α-helix | 463-465 | 3 | |
| β-strand | 468-474 | 7 | 7 |
| β-strand | 479-485 | 7 | 7 |
| β-strand | 490-494 | 5 | 7 |
| α-helix | 502-520 | 19 | |
| α-helix | 526-528 | 3 | |
| β-strand | 530-533 | 4 | 7 |
| α-helix | 540-542 | 3 | |
| α-helix | 548-560 | 13 | |
| α-helix | 569-571 | 3 | |
| α-helix | 572-585 | 14 | |
Chain D: 2 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 18-22 | 5 | 8 |
| β-strand | 28-32 | 5 | 8 |
| α-helix | 40-50 | 11 | |
| α-helix | 54-56 | 3 | |
| β-strand | 57-61 | 5 | 8 |
| β-strand | 64-65 | 2 | 8 |
| β-strand | 81-87 | 7 | 8 |
| β-strand | 90 | 1 | 6 |
Chain E: 16 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 370-380 | 11 | |
| β-strand | 388-392 | 5 | 9 |
| β-strand | 395-398 | 4 | 9 |
| α-helix | 399-402 | 4 | |
| α-helix | 403-405 | 3 | |
| α-helix | 409-410 | 2 | |
| β-strand | 411-412 | 2 | 10 |
| α-helix | 413-430 | 18 | |
| α-helix | 432-434 | 3 | |
| β-strand | 435-437 | 3 | 11 |
| α-helix | 442-449 | 8 | |
| α-helix | 451-454 | 4 | |
| α-helix | 455-458 | 4 | |
| α-helix | 463-465 | 3 | |
| β-strand | 468-474 | 7 | 11 |
| β-strand | 479-485 | 7 | 11 |
| β-strand | 490-494 | 5 | 11 |
| α-helix | 502-519 | 18 | |
| α-helix | 526-528 | 3 | |
| β-strand | 530-532 | 3 | 11 |
| α-helix | 540-542 | 3 | |
| α-helix | 548-559 | 12 | |
| α-helix | 569-571 | 3 | |
| α-helix | 572-585 | 14 | |
Chain F: 2 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 17-23 | 7 | 12 |
| β-strand | 28-33 | 6 | 12 |
| α-helix | 40-48 | 9 | |
| β-strand | 57-61 | 5 | 12 |
| β-strand | 64-65 | 2 | 12 |
| β-strand | 82-87 | 6 | 12 |
| α-helix | 88 | 1 | |
| β-strand | 90-91 | 2 | 10 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Sentrin-specific protease 2 | A, C, E | protein | 232 | Homo sapiens | Q9HC62 (AlphaFold model) |
| Small ubiquitin-related modifier 3 precursor | B, D, F | protein | 94 | Homo sapiens | P55854 (AlphaFold model) |
Sequence of entity 1 (A, C, E), FASTA
>2IO1_1 Sentrin-specific protease 2 (chains A, C, E)
GSHMASDLLELTEDMEKEISNALGHGPQDEILSSAFKLRITRGDIQTLKNYHWLNDEVIN
FYMNLLVERNKKQGYPALHVFSTFFYPKLKSGGYQAVKRWTKGVNLFEQEIILVPIHRKV
HWSLVVIDLRKKCLKYLDSMGQKGHRICEILLQYLQDESKTKRNSDLNLLEWTHHSMKPH
EIPQQLNGSDSGMFTCKYADYISRDKPITFTQHQMPLFRKKMVWEILHQQLL
Sequence of entity 2 (B, D, F), FASTA
>2IO1_2 Small ubiquitin-related modifier 3 precursor (chains B, D, F)
GSHMNDHINLKVAGQDGSVVQFKIKRHTPLSKLMKAYCERQGLSMRQIRFRFDGQPINET
DTPAQLEMEDEDTIDVFQQQTGGVPESSLAGHSF
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
- 2IO0 2.3 Å, Crystal structure of human Senp2 in complex with preSUMO-2
- 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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