Research workbench
Crystal structure of ubiquitin carboxy-terminal hydrolase L1 (uch-L1)
Analyse Crystal structure of ubiquitin carboxy-terminal hydrolase L1 (uch-L1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ETL
- Type
- protein
- Length
- 446 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ubiquitin carboxyl-terminal hydrolase isozyme L1
- EC
- 3.4.19.12, 6.-.-.-
- UniProt
- P09936
- Ligands
- CL
- Pockets
- 4 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ubiquitin carboxyl-terminal hydrolase isozyme L1 (EC 3.4.19.12, 6.-.-.-) | protein | 223 | 35% helix, 20% strand | P09936 |
Ligands and binding sites
- CL · Chloride ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 320 | 0.65 | 0.81 | 47 | empty |
| 2 | 215 | 0.54 | 0.78 | 24 | CL |
| 3 | 124 | 0.47 | 0.79 | 24 | CL |
| 4 | 110 | 0.42 | 0.77 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 542 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 2ETL · Crystal Structure of Ubiquitin Carboxy-terminal Hydrolase L1 (UCH-L1) · the same entry in another collection · chain A against A, TM-score 1.00
- P09936 · AlphaFold monomer V2.0 prediction for ubiquitin carboxyl-terminal hydrolase isozyme L1… · a predicted model of the same protein · chain A against A, TM-score 0.97
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P09936
- Elsewhere: RCSB PDB 2ETL · PDBe 2ETL · UniProt P09936
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