MolNFT v1 · #17081 · protein
Structure of caenorhabditis elegans ced-9
1OHU · Apoptosis regulator ced-9: “Structure of caenorhabditis elegans ced-9”. X-ray diffraction, 3 pockets (best druggability 0.60). MolNFT v1 #17081 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1OHU
- Type
- protein
- Length
- 333 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Apoptosis regulator ced-9
- UniProt
- P41958
- Pockets
- 3 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 70% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Apoptosis regulator ced-9 | protein | 165 | 70% helix, 0% strand | P41958 |
| B | Apoptosis regulator ced-9 | protein | 168 | 71% helix, 0% strand | P41958 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 351 | 0.60 | 0.77 | 29 | empty |
| 2 | 53 | 0.34 | 0.78 | 11 | empty |
| 3 | 51 | 0.30 | 0.75 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 304 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 18 modified (engineered).
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 P41958
- Elsewhere: RCSB PDB 1OHU · PDBe 1OHU · UniProt P41958
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.