Research workbench
Crystal structure of trichoplusia ni CPV15 polyhedra
Analyse Crystal structure of trichoplusia ni CPV15 polyhedra in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5A98
- Type
- protein
- Length
- 235 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polyhedrin
- UniProt
- Q9ELS6
- Ligands
- ATP, MG
- Pockets
- 5 · best druggability 0.42
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyhedrin | protein | 235 | 23% helix, 25% strand | Q9ELS6 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A
- MG · Magnesium ion · metal · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 140 | 0.42 | 0.75 | 17 | empty |
| 2 | 133 | 0.38 | 0.74 | 23 | empty |
| 3 | 60 | 0.37 | 0.79 | 19 | empty |
| 4 | 94 | 0.37 | 0.75 | 22 | empty |
| 5 | 55 | 0.26 | 0.73 | 19 | empty |
Compared structures
- 5A98 · Crystal structure of Trichoplusia ni CPV15 polyhedra · 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 Q9ELS6
- Elsewhere: RCSB PDB 5A98 · PDBe 5A98 · UniProt Q9ELS6
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