Research workbench
Crystal structure of the complex of xiap-BIR2 and caspase 3
Analyse Crystal structure of the complex of xiap-BIR2 and caspase 3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1I3O
- Type
- protein
- Length
- 693 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Caspase 3; Baculoviral iap repeat-containing protein 4
- EC
- 3.4.22.-
- UniProt
- P42574, P98170
- Ligands
- ZN
- Pockets
- 7 · best druggability 0.63
Structure
x-ray diffraction · 5 distinct chains · 30% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Caspase 3 (EC 3.4.22.-) | protein | 143 | 26% helix, 31% strand | P42574 |
| B, D | Caspase 3 (EC 3.4.22.-) | protein | 101 | 31% helix, 17% strand | P42574 |
| C | Caspase 3 (EC 3.4.22.-) | protein | 144 | 26% helix, 31% strand | P42574 |
| E | Baculoviral iap repeat-containing protein 4 | protein | 111 | 32% helix, 12% strand | P98170 |
| F | Baculoviral iap repeat-containing protein 4 | protein | 93 | 39% helix, 14% strand | P98170 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 375 | 0.63 | 0.78 | 36 | empty |
| 2 | 281 | 0.53 | 0.75 | 32 | empty |
| 3 | 51 | 0.51 | 0.88 | 20 | empty |
| 4 | 72 | 0.35 | 0.77 | 15 | empty |
| 5 | 82 | 0.32 | 0.74 | 14 | empty |
Interfaces
12 interfaces between chains.
- C–D · 2133 Ų buried · 30 hydrogen bonds · protein-protein
- A–B · 2119 Ų buried · 33 hydrogen bonds · protein-protein
- B–D · 1597 Ų buried · 24 hydrogen bonds · protein-protein
- D–F · 911 Ų buried · 16 hydrogen bonds · protein-protein
- B–E · 906 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
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 P42574
- Every structure of UniProt P98170
- Elsewhere: RCSB PDB 1I3O · PDBe 1I3O · UniProt P42574 · UniProt P98170
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.