Research workbench
Bacteriophage HK97 pepsin-treated expansion intermediate IV
Analyse Bacteriophage HK97 pepsin-treated expansion intermediate IV in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FSY
- Type
- protein
- Length
- 1,899 residues
- Chains
- 7
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Major capsid protein
- UniProt
- P49861
- Pockets
- 20 · best druggability 0.74
Structure
x-ray diffraction · 3 distinct chains · 26% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Major capsid protein | protein | 280 | 24% helix, 33% strand | P49861 |
| F | Major capsid protein | protein | 256 | 26% helix, 35% strand | P49861 |
| G | Major capsid protein | protein | 243 | 27% helix, 28% strand | P49861 |
Pockets
20 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 788 | 0.74 | 0.79 | 57 | empty |
| 2 | 282 | 0.59 | 0.78 | 28 | empty |
| 3 | 276 | 0.58 | 0.77 | 26 | empty |
| 4 | 293 | 0.58 | 0.77 | 27 | empty |
| 5 | 263 | 0.58 | 0.78 | 26 | empty |
Interfaces
17 interfaces between chains.
- B–C · 2494 Ų buried · 38 hydrogen bonds · protein-protein
- C–D · 2492 Ų buried · 35 hydrogen bonds · protein-protein
- D–E · 2486 Ų buried · 41 hydrogen bonds · protein-protein
- E–F · 2470 Ų buried · 34 hydrogen bonds · protein-protein
- A–B · 2434 Ų buried · 34 hydrogen bonds · protein-protein
Compared structures
- 2FSY · Bacteriophage HK97 Pepsin-treated Expansion Intermediate IV · the same entry in another collection · chain E against E, 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 P49861
- Elsewhere: RCSB PDB 2FSY · PDBe 2FSY · UniProt P49861
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