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The 2.7 ångström resolution crystal structure of a mutated baculovirus P35 after caspase cleavage
Analyse The 2.7 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
- 1I3S
- Type
- protein
- Length
- 846 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Early 35 kda protein
- UniProt
- P08160
- Pockets
- 4 · best druggability 0.62
Structure
x-ray diffraction · 3 distinct chains · 19% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Early 35 kda protein | protein | 283 | 19% helix, 42% strand | P08160 |
| B | Early 35 kda protein | protein | 281 | 20% helix, 41% strand | P08160 |
| C | Early 35 kda protein | protein | 282 | 19% helix, 41% strand | P08160 |
Ligands and binding sites
- DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 238 | 0.62 | 0.81 | 32 | DTT |
| 2 | 222 | 0.60 | 0.81 | 27 | DTT |
| 3 | 227 | 0.58 | 0.79 | 27 | DTT |
| 4 | 104 | 0.36 | 0.74 | 26 | empty |
Interfaces
2 interfaces between chains.
- B–C · 263 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 227 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 covalent (additive adduct).
Compared structures
- 1I3S · The 2.7 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 1I3S · PDBe 1I3S · UniProt P08160
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