Structure of human Senp2 in complex with SUMO-1. Determined by X-ray diffraction at 2.8 Å resolution. Released 14 Sept 2004.
Explore 1TGZ in 3D Show helices and sheets RCSB PDB PDBe
1TGZ contains 16 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 370-380 | 11 | |
| β-strand | 388-392 | 5 | 1 |
| β-strand | 395-398 | 4 | 1 |
| α-helix | 399-403 | 5 | |
| 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 | 502-519 | 18 | |
| α-helix | 526-528 | 3 | |
| β-strand | 530-533 | 4 | 3 |
| α-helix | 548-559 | 12 | |
| α-helix | 569-571 | 3 | |
| α-helix | 572-584 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 22-28 | 7 | 4 |
| β-strand | 35-38 | 4 | 4 |
| α-helix | 45-53 | 9 | |
| α-helix | 59-61 | 3 | |
| β-strand | 62-66 | 5 | 4 |
| β-strand | 69-70 | 2 | 4 |
| α-helix | 77-80 | 4 | |
| β-strand | 87-92 | 6 | 4 |
| β-strand | 95-96 | 2 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sentrin-specific protease 2 | A | protein | 226 | Homo sapiens | Q9HC62 (AlphaFold model) |
| Ubiquitin-like protein SMT3C | B | protein | 80 | Homo sapiens | P63165 (AlphaFold model) |
>1TGZ_1 Sentrin-specific protease 2 (chains A) DLLELTEDMEKEISNALGHGPQDEILSSAFKLRITRGDIQTLKNYHWLNDEVINFYMNLL VERNKKQGYPALHVFSTFFYPKLKSGGYQAVKRWTKGVNLFEQEIILVPIHRKVHWSLVV IDLRKKCLKYLDSMGQKGHRICEILLQYLQDESKTKRNSDLNLLEWTHHSMKPHEIPQQL NGSDCGMFTCKYADYISRDKPITFTQHQMPLFRKKMVWEILHQQLL
>1TGZ_2 Ubiquitin-like protein SMT3C (chains B) EGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTP KELGMEEEDVIEVYQEQTGG
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:
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