13CU: Ubiquitin carboxyl-terminal hydrolase isozyme L3

Crystal structure of covalent inhibitor 2-chloro-N-(3-((pyridin-2-ylthio)methyl)phenyl)acetamide bound to Ubiquitin C-terminal Hydrolase-L3. Determined by X-ray diffraction at 1.95 Å resolution. Released 26 Aug 2026.

Method
X-ray diffraction
Resolution
1.95 Å
Organism
Homo sapiens
Chains
3
Atoms
5,233
Mol. weight
81.58 kDa
Ligands
A1DFC
Released
26 Aug 2026

Explore 13CU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

13CU contains 30 α-helices and 24 β-strands across 3 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: 10 helices, 8 β-strands

ElementResiduesLengthSheet
α-helix6-83
α-helix13-2210
β-strand2511
β-strand29-3352
α-helix39-424
β-strand49-5792
α-helix60-7617
α-helix95-10511
α-helix108-1103
β-strand11311
α-helix118-1258
α-helix131-1399
α-helix142-1443
β-strand168-17692
β-strand179-18352
β-strand191-19552
α-helix201-21515
β-strand223-22972
Chain B: 11 helices, 8 β-strands
ElementResiduesLengthSheet
α-helix13-2210
β-strand2513
β-strand29-3354
α-helix39-424
β-strand49-5794
α-helix60-7617
α-helix95-10511
α-helix108-1103
β-strand11313
α-helix118-1269
α-helix131-14010
α-helix142-1443
α-helix146-1472
α-helix148-1514
β-strand168-17694
β-strand179-18354
β-strand191-19554
α-helix201-21515
β-strand223-22974
Chain C: 9 helices, 8 β-strands
ElementResiduesLengthSheet
α-helix13-2210
β-strand2515
β-strand29-3356
α-helix39-424
β-strand49-5796
α-helix60-7617
α-helix95-10511
α-helix108-1103
β-strand11315
α-helix118-1269
α-helix131-1399
α-helix142-1443
β-strand168-17696
β-strand179-18356
β-strand191-19556
α-helix201-21515
β-strand223-22976

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ubiquitin carboxyl-terminal hydrolase isozyme L3A, B, Cprotein238Homo sapiensP15374 (AlphaFold model)
Sequence of entity 1 (A, B, C), FASTA
>13CU_1 Ubiquitin carboxyl-terminal hydrolase isozyme L3 (chains A, B, C)
GPLGSPEFMEGQRWLPLEANPEVTNQFLKQLGLHPNWQFVDVYGMDPELLSMVPRPVCAV
LLLFPITEKYEVFRTEEEEKIKSQGQDVTSSVYFMKQTISNACGTIGLIHAIANNKDKMH
FESGSTLKKFLEESVSMSPEERARYLENYDAIRVTHETSAHEGQTEAPSIDEKVDLHFIA
LVHVDGHLYELDGRKPFPINHGETSDETLLEDAIEVCKKFMERDPDELRFNAIALSAA

Ligands and cofactors

IDNameFormulaCopies
A1DFCN-(3-{[(pyridin-2-yl)sulfanyl]methyl}phenyl)propanamideC14 H13 Cl N2 O S2

Primary citation

Identification, optimization, and structural elucidation of chloroacetamide scaffold as covalent inhibitors for Ubiquitin C-terminal Hydrolase L3. Beeralingappa, N.C., Lu, M., Patel, R. et al. bioRxiv (2026). DOI 10.64898/2026.05.26.727856

Other PDB entries of the same protein (UniProt P15374 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 13CU directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.