SUMO protease Ulp1 with the catalytic cysteine oxidized to a sulfenic acid. Determined by X-ray diffraction at 2.1 Å resolution. Released 31 Jul 2007.
Explore 2HKP in 3D Show helices and sheets RCSB PDB PDBe
2HKP contains 13 α-helices and 7 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 405-408 | 4 | |
| α-helix | 409-420 | 12 | |
| β-strand | 426-430 | 5 | 1 |
| β-strand | 433-436 | 4 | 1 |
| α-helix | 437-440 | 4 | |
| α-helix | 441-443 | 3 | |
| α-helix | 451-463 | 13 | |
| β-strand | 468-470 | 3 | 2 |
| α-helix | 474-482 | 9 | |
| α-helix | 484-487 | 4 | |
| α-helix | 490-493 | 4 | |
| α-helix | 498-500 | 3 | |
| β-strand | 503-510 | 8 | 2 |
| β-strand | 514-521 | 8 | 2 |
| β-strand | 526-530 | 5 | 2 |
| α-helix | 539-555 | 17 | |
| β-strand | 565-568 | 4 | 2 |
| α-helix | 572-574 | 3 | |
| α-helix | 580-592 | 13 | |
| α-helix | 601-616 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin-like-specific protease 1 | A | protein | 221 | Saccharomyces cerevisiae | Q02724 (AlphaFold model) |
>2HKP_1 Ubiquitin-like-specific protease 1 (chains A) GSLVPELNEKDDDQVQKALASRENTQLMNRDNIEITVRDFKTLAPRRWLNDTIIEFFMKY IEKSTPNTVAFNSFFYTNLSERGYQGVRRWMKRKKTQIDKLDKIFTPINLNQSHWALGII DLKKKTIGYVDSLSNGPNAMSFAILTDLQKYVMEESKHTIGEDFDLIHLDCPQQPNGYDC GIYVCMNTLYGSADAPLDFDYKDAIRMRRFIAHLILTDALK
Molecular basis of the redox regulation of SUMO proteases: a protective mechanism of intermolecular disulfide linkage against irreversible sulfhydryl oxidation. Xu, Z., Lam, L.S.M., Lam, L.H. et al. FASEB J (2008) 22:127-137. DOI 10.1096/fj.06-7871com · PubMed
Other PDB entries of the same protein (UniProt Q02724 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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