MolNFT v1 · #2118 · protein
Bm-40, FS/EC domain pair
1BMO: “Bm-40, FS/EC domain pair”. X-ray diffraction, 2 ligands (NAG, CA), 8 pockets (best druggability 0.55). MolNFT v1 #2118 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1BMO
- Type
- protein
- Length
- 466 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bm-40
- UniProt
- P09486
- Ligands
- NAG, CA
- Pockets
- 8 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Bm-40 | protein | 233 | 46% helix, 11% strand | P09486 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B
- CA · Calcium ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 232 | 0.55 | 0.78 | 25 | empty |
| 2 | 219 | 0.55 | 0.78 | 24 | empty |
| 3 | 162 | 0.49 | 0.77 | 35 | empty |
| 4 | 92 | 0.46 | 0.80 | 19 | empty |
| 5 | 79 | 0.45 | 0.81 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 712 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 disulfide, 2 glycan (disulfide, N-glycosylation).
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 P09486
- Elsewhere: RCSB PDB 1BMO · PDBe 1BMO · UniProt P09486
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.