Research workbench
Solution structure of the first uba domain in the human ubiquitin specific protease 5 (isopeptidase 5)
Analyse Solution structure of the first uba domain in the human ubiquitin specific… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2DAG
- Type
- protein
- Length
- 74 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ubiquitin carboxyl-terminal hydrolase 5
- EC
- 3.1.2.15
- UniProt
- P45974
Structure
solution nmr · 1 distinct chain · 43% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ubiquitin carboxyl-terminal hydrolase 5 (EC 3.1.2.15) | protein | 74 | 43% helix, 0% strand | P45974 |
Compared structures
- 2DAG · Solution Structure of the First UBA Domain in the Human Ubiquitin Specific Protease 5… · 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 A against A, TM-score 0.62
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 2DAG · PDBe 2DAG · UniProt P45974
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