2HL9: Ubiquitin-like-specific protease 1

SUMO protease Ulp1 with the catalytic cysteine oxidized to a sulfonic acid. Determined by X-ray diffraction at 1.9 Å resolution. Released 31 Jul 2007.

Method
X-ray diffraction
Resolution
1.9 Å
Organism
Saccharomyces cerevisiae
Chains
1
Atoms
1,884
Mol. weight
25.7 kDa
Released
31 Jul 2007

Explore 2HL9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2HL9 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.

Chain A: 13 helices, 7 β-strands

ElementResiduesLengthSheet
α-helix405-4084
α-helix409-42012
β-strand426-42831
β-strand435-43621
α-helix437-4404
α-helix441-4433
α-helix448-4503
α-helix451-46313
β-strand468-47032
α-helix474-48714
α-helix492-4943
α-helix498-5003
β-strand503-51082
β-strand514-52182
β-strand526-53052
α-helix539-55517
β-strand565-56952
α-helix572-5743
α-helix580-59213
α-helix601-61616

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ubiquitin-like-specific protease 1Aprotein221Saccharomyces cerevisiaeQ02724 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2HL9_1 Ubiquitin-like-specific protease 1 (chains A)
GSLVPELNEKDDDQVQKALASRENTQLMNRDNIEITVRDFKTLAPRRWLNDTIIEFFMKY
IEKSTPNTVAFNSFFYTNLSERGYQGVRRWMKRKKTQIDKLDKIFTPINLNQSHWALGII
DLKKKTIGYVDSLSNGPNAMSFAILTDLQKYVMEESKHTIGEDFDLIHLDCPQQPNGYDC
GIYVCMNTLYGSADAPLDFDYKDAIRMRRFIAHLILTDALK

Primary citation

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:

Browse structure collections

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