Research workbench
Hepatitis B core protein + gsllgrmkga
Analyse Hepatitis B core protein + gsllgrmkga in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OD6
- Type
- protein
- Length
- 593 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Capsid protein; Inhibitory peptide P2 (gsllgrmkga)
- UniProt
- P03146
- Pockets
- 8 · best druggability 0.78
Structure
electron microscopy · 4 distinct chains · 67% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Capsid protein | protein | 150 | 66% helix, 1% strand | P03146 |
| A | Capsid protein | protein | 143 | 68% helix, 0% strand | P03146 |
| C, D | Capsid protein | protein | 144 | 69% helix, 1% strand | P03146 |
| F, E | Inhibitory peptide P2 (gsllgrmkga) | protein | 6 | 0% helix, 0% strand | — |
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 146 | 0.78 | 0.95 | 27 | empty |
| 2 | 139 | 0.65 | 0.87 | 36 | empty |
| 3 | 111 | 0.57 | 0.84 | 19 | empty |
| 4 | 67 | 0.52 | 0.85 | 17 | empty |
| 5 | 52 | 0.52 | 0.87 | 15 | empty |
Interfaces
7 interfaces between chains.
- B–A · 2003 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 1999 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 1000 Ų buried · 12 hydrogen bonds · protein-protein
- D–E · 223 Ų buried · 1 hydrogen bond · protein-protein
- B–F · 218 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 7OD6 · Hepatitis B core protein + GSLLGRMKGA · the same entry in another collection · chain B against B, 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 P03146
- Elsewhere: RCSB PDB 7OD6 · PDBe 7OD6 · UniProt P03146
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