MolNFT v1 · #52179 · protein
Structure of a conserved dimerisation domain within FBOX7 and PI31
2VT8 · Proteasome inhibitor PI31 subunit: “Structure of a conserved dimerisation domain within FBOX7 and PI31”. X-ray diffraction, 2 pockets (best druggability 0.46). MolNFT v1 #52179 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 2VT8
- Type
- protein
- Length
- 286 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proteasome inhibitor PI31 subunit
- UniProt
- Q92530
- Pockets
- 2 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proteasome inhibitor PI31 subunit | protein | 143 | 32% helix, 29% strand | Q92530 |
| B | Proteasome inhibitor PI31 subunit | protein | 143 | 32% helix, 29% strand | Q92530 |
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 | 76 | 0.46 | 0.81 | 19 | empty |
| 2 | 139 | 0.43 | 0.75 | 31 | empty |
Interfaces
1 interface between chains.
- A–B · 320 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (oxidation).
Compared structures
- 2VT8 · Structure of a conserved dimerisation domain within Fbox7 and PI31 · the same entry in another collection · chain A against A, TM-score 1.00
- Q92530 · AlphaFold monomer V2.0 prediction for proteasome inhibitor PI31 subunit (Q92530) · a predicted model of the same protein · chain B 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 Q92530
- Elsewhere: RCSB PDB 2VT8 · PDBe 2VT8 · UniProt Q92530
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