Research workbench
The catalytic domain of human deubiquitinase duba in complex with ubiquitin aldehyde
Analyse The catalytic domain of human deubiquitinase duba in complex with ubiquitin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TMP
- Type
- protein
- Length
- 961 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q96G74, P0CG48
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 166 | — | Q96G74 |
| B, D, F, H | — | protein | 76 | — | P0CG48 |
| C | — | protein | 168 | — | Q96G74 |
| E | — | protein | 169 | — | Q96G74 |
| G | — | protein | 154 | — | Q96G74 |
Compared structures
- 3TMP · The catalytic domain of human deubiquitinase DUBA in complex with ubiquitin aldehyde · the same entry in another collection · chain H against H, TM-score 1.00
- Q96G74 · AlphaFold monomer V2.0 prediction for otu domain-containing protein 5 (Q96G74) · a predicted model of the same protein · chain C against A, TM-score 0.98
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 Q96G74
- Every structure of UniProt P0CG48
- Elsewhere: RCSB PDB 3TMP · PDBe 3TMP · UniProt Q96G74 · UniProt P0CG48
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