13CV: Ubiquitin carboxyl-terminal hydrolase isozyme L3

Crystal structure of covalent inhibitor 3-(2-chloroacetamido)-N-(pyridin-2-yl)benzamide bound to Ubiquitin C-terminal Hydrolase-L3. Determined by X-ray diffraction at 1.94 Å resolution. Released 26 Aug 2026.

Method
X-ray diffraction
Resolution
1.94 Å
Organism
Homo sapiens
Chains
4
Atoms
7,205
Mol. weight
108.62 kDa
Ligands
A1DFD
Released
26 Aug 2026

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

Secondary structure: helices and β-sheets

13CV contains 39 α-helices and 32 β-strands across 4 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-helix9-113
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-helix131-14010
α-helix162-1643
β-strand168-17692
β-strand179-18352
β-strand191-19552
α-helix201-21515
β-strand223-22972
Chain B: 9 helices, 8 β-strands
ElementResiduesLengthSheet
α-helix9-113
α-helix13-2210
β-strand2513
β-strand29-3464
α-helix39-424
β-strand49-5794
α-helix60-7617
α-helix95-10511
α-helix108-1103
β-strand11313
α-helix118-1269
α-helix131-14010
β-strand168-17694
β-strand179-18354
β-strand191-19554
α-helix201-21515
β-strand223-22974
Chain C: 10 helices, 8 β-strands
ElementResiduesLengthSheet
α-helix9-113
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-helix1141
α-helix118-1269
α-helix131-14010
β-strand168-17696
β-strand179-18356
β-strand191-19556
α-helix201-21515
β-strand223-22976
Chain D: 10 helices, 8 β-strands
ElementResiduesLengthSheet
α-helix9-113
α-helix13-2210
β-strand2517
β-strand29-3468
α-helix39-424
β-strand49-5798
α-helix60-7617
α-helix95-10511
β-strand11317
α-helix118-1258
α-helix131-14010
α-helix159-1613
α-helix162-1643
β-strand168-17698
β-strand179-18358
β-strand191-19558
α-helix201-21414
β-strand223-22978

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ubiquitin carboxyl-terminal hydrolase isozyme L3A, B, C, Dprotein235Homo sapiensP15374 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>13CV_1 Ubiquitin carboxyl-terminal hydrolase isozyme L3 (chains A, B, C, D)
GPLGSMEGQRWLPLEANPEVTNQFLKQLGLHPNWQFVDVYGMDPELLSMVPRPVCAVLLL
FPITEKYEVFRTEEEEKIKSQGQDVTSSVYFMKQTISNACGTIGLIHAIANNKDKMHFES
GSTLKKFLEESVSMSPEERARYLENYDAIRVTHETSAHEGQTEAPSIDEKVDLHFIALVH
VDGHLYELDGRKPFPINHGETSDETLLEDAIEVCKKFMERDPDELRFNAIALSAA

Ligands and cofactors

IDNameFormulaCopies
A1DFD3-(2-chloroacetamido)-N-(pyridin-2-yl)benzamideC14 H12 Cl N3 O24

Water and common crystallization additives (SO4) are not listed.

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:

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