Research workbench
The crystal structure of obelin from obelia longissima bound with V- coelenterazine
Analyse The crystal structure of obelin from obelia longissima bound with V… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7O3U
- Type
- protein
- Length
- 189 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Obelin
- UniProt
- Q27709
- Ligands
- V1W, CA
- Pockets
- 1 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 60% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Obelin | protein | 189 | 60% helix, 5% strand | Q27709 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 201 | 0.83 | 0.96 | 30 | V1W |
Compared structures
- 7O3U · The crystal structure of obelin from Obelia longissima bound with v-coelenterazine · the same entry in another collection · chain A against A, TM-score 1.00
- Q27709 · AlphaFold monomer V2.0 prediction for obelin (Q27709) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q27709
- Elsewhere: RCSB PDB 7O3U · PDBe 7O3U · UniProt Q27709
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