MolNFT v1 · #143055 · protein
Structure of bmval-1
6ANY · BM4233, isoform B: “Structure of bmval-1”. X-ray diffraction, 4 ligands (NAG, FUC, BMA), 1 pocket (best druggability 0.33). MolNFT v1 #143055 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6ANY
- Type
- protein
- Length
- 206 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BM4233, isoform B
- UniProt
- O44932
- Ligands
- NAG, FUC, BMA, SO4
- Pockets
- 1 · best druggability 0.33
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | BM4233, isoform B | protein | 206 | 34% helix, 20% strand | O44932 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
- FUC · alpha-L-fucopyranose · sugar · 2 copies · chains A
- BMA · beta-D-mannopyranose · sugar
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 69 | 0.33 | 0.75 | 14 | empty |
Modifications
Observed in the structure: 5 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
- 6ANY · Structure of BmVAL-1 · the same entry in another collection · chain A against A, TM-score 1.00
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 O44932
- Elsewhere: RCSB PDB 6ANY · PDBe 6ANY · UniProt O44932
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