Research workbench
Structure of bmnpv ORF075 (P33)
Analyse Structure of bmnpv ORF075 (P33) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UST
- Type
- protein
- Length
- 247 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acmnpv ORF92
- UniProt
- O92452
- Ligands
- FAD
- Pockets
- 5 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 68% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acmnpv ORF92 | protein | 247 | 68% helix, 2% strand | O92452 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 140 | 0.62 | 0.85 | 20 | FAD |
| 2 | 90 | 0.53 | 0.84 | 19 | empty |
| 3 | 185 | 0.51 | 0.77 | 25 | empty |
| 4 | 88 | 0.38 | 0.76 | 17 | empty |
| 5 | 58 | 0.28 | 0.73 | 13 | empty |
Modifications
Observed in the structure: 15 modified, 2 disulfide (engineered, disulfide).
Compared structures
- 3UST · Structure of BmNPV ORF075 (p33) · 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 O92452
- Elsewhere: RCSB PDB 3UST · PDBe 3UST · UniProt O92452
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