MolNFT v1 · #483 · protein
Dominant B-cell epitope from the PRES2 region of hepatitis B virus in the form of an inserted peptide segment in maltodextrin-binding protein
1A7L · Male-B363: “Dominant B-cell epitope from the PRES2 region of hepatitis B virus in the form of an inserted peptide segment…”. X-ray diffraction, 1 ligand (GLC), 9 pockets (best druggability 0.81). MolNFT v1 #483 on GenesisL1: 3D…
- PDB
- 1A7L
- Type
- protein
- Length
- 1,114 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Male-B363
- UniProt
- P02928
- Ligands
- GLC
- Pockets
- 9 · best druggability 0.81
Structure
x-ray diffraction · 3 distinct chains · 44% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Male-B363 | protein | 380 | 44% helix, 17% strand | P02928 |
| B | Male-B363 | protein | 372 | 44% helix, 20% strand | P02928 |
| C | Male-B363 | protein | 362 | 45% helix, 20% strand | P02928 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 6 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 835 | 0.81 | 0.84 | 70 | GLC |
| 2 | 298 | 0.72 | 0.85 | 27 | GLC |
| 3 | 361 | 0.70 | 0.82 | 35 | GLC |
| 4 | 479 | 0.63 | 0.76 | 47 | empty |
| 5 | 229 | 0.49 | 0.74 | 26 | empty |
Interfaces
3 interfaces between chains.
- A–B · 406 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 234 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 59 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1A7L · Dominant B-cell epitope from the PRES2 region of hepatitis B virus in the form of an… · 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 P02928
- Elsewhere: RCSB PDB 1A7L · PDBe 1A7L · UniProt P02928
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