MolNFT v1 · #51413 · protein
The structure of the BEM1P px domain
2V6V · Bud emergence protein 1: “The structure of the BEM1P px domain”. X-ray diffraction, 2 pockets (best druggability 0.38). MolNFT v1 #51413 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2V6V
- Type
- protein
- Length
- 270 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bud emergence protein 1
- UniProt
- P29366
- Pockets
- 2 · best druggability 0.38
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bud emergence protein 1 | protein | 135 | 31% helix, 24% strand | P29366 |
| B | Bud emergence protein 1 | protein | 135 | 33% helix, 23% strand | P29366 |
Ligands and binding sites
- DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · chains A
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 | 98 | 0.38 | 0.75 | 15 | empty |
| 2 | 86 | 0.32 | 0.73 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 448 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
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 P29366
- Elsewhere: RCSB PDB 2V6V · PDBe 2V6V · UniProt P29366
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.