MolNFT v1 · #37519 · protein
Structure of the znf ubp domain from deubiquitinating enzyme isopeptidase T (isot)
2G43 · Ubiquitin carboxyl-terminal hydrolase 5: “Structure of the znf ubp domain from deubiquitinating enzyme isopeptidase T (isot)”. X-ray diffraction, 2 ligands (ZN, UNX), 2 pockets (best druggability 0.38). MolNFT v1 #37519 on…
- PDB
- 2G43
- Type
- protein
- Length
- 230 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ubiquitin carboxyl-terminal hydrolase 5
- EC
- 3.1.2.15
- UniProt
- P45974
- Ligands
- ZN, UNX
- Pockets
- 2 · best druggability 0.38
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ubiquitin carboxyl-terminal hydrolase 5 (EC 3.1.2.15) | protein | 117 | 13% helix, 20% strand | P45974 |
| B | Ubiquitin carboxyl-terminal hydrolase 5 (EC 3.1.2.15) | protein | 113 | 13% helix, 19% strand | P45974 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.38 | 0.78 | 13 | empty |
| 2 | 52 | 0.32 | 0.77 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 94 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2G43 · Structure of the ZNF UBP domain from deubiquitinating enzyme isopeptidase T (IsoT) · the same entry in another collection · chain A against A, TM-score 1.00
- P45974 · AlphaFold monomer V2.0 prediction for ubiquitin carboxyl-terminal hydrolase 5 (P45974) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 P45974
- Elsewhere: RCSB PDB 2G43 · PDBe 2G43 · UniProt P45974
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