Research workbench
Hepatitis B core protein mutant F97L with bound gsllgrmkga
Analyse Hepatitis B core protein mutant F97L with bound gsllgrmkga in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OEV
- Type
- protein
- Length
- 593 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Capsid protein; Gsllgrmkga
- UniProt
- P03146
- Pockets
- 10 · best druggability 0.78
Structure
electron microscopy · 4 distinct chains · 65% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Capsid protein | protein | 150 | 65% helix, 1% strand | P03146 |
| A | Capsid protein | protein | 143 | 66% helix, 0% strand | P03146 |
| C, D | Capsid protein | protein | 144 | 65% helix, 1% strand | P03146 |
| E, F | Gsllgrmkga | protein | 6 | 0% helix, 0% strand | — |
Pockets
10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 155 | 0.78 | 0.94 | 29 | empty |
| 2 | 70 | 0.67 | 0.94 | 22 | empty |
| 3 | 57 | 0.65 | 0.94 | 19 | empty |
| 4 | 134 | 0.64 | 0.86 | 23 | empty |
| 5 | 65 | 0.61 | 0.91 | 16 | empty |
Interfaces
8 interfaces between chains.
- B–A · 1976 Ų buried · 12 hydrogen bonds · protein-protein
- C–D · 1925 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 1015 Ų buried · 17 hydrogen bonds · protein-protein
- A–F · 225 Ų buried · 4 hydrogen bonds · protein-protein
- B–F · 213 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 7OEV · Hepatitis B core protein mutant F97L with bound 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 7OEV · PDBe 7OEV · UniProt P03146
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