Research workbench
The 3.1 ångström resolution crystal structure of a mutated baculovirus P35 after caspase cleavage
Analyse The 3.1 ångström resolution crystal structure of a mutated baculovirus P35… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1I3P
- Type
- protein
- Length
- 274 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Early 35 kda protein
- UniProt
- P08160
- Pockets
- 2 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 21% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Early 35 kda protein | protein | 274 | 21% helix, 39% strand | P08160 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 245 | 0.59 | 0.79 | 29 | empty |
| 2 | 83 | 0.35 | 0.75 | 16 | empty |
Compared structures
- 1I3P · The 3.1 ångström resolution crystal structure of a mutated baculovirus P35 after caspase… · 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 P08160
- Elsewhere: RCSB PDB 1I3P · PDBe 1I3P · UniProt P08160
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