Research workbench
Crystal structure of W92F obelin mutant from obelia longissima at 1.72 ångström resolution
Analyse Crystal structure of W92F obelin mutant from obelia longissima at 1.72 ångström… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JF2
- Type
- protein
- Length
- 190 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Obelin
- UniProt
- Q27709
- Ligands
- CZH
- Pockets
- 1 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 59% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Obelin | protein | 190 | 59% helix, 3% strand | Q27709 |
Ligands and binding sites
- CZH · C2-hydroperoxy-coelenterazine · ligand · chains A
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 | 0.84 | 0.97 | 31 | CZH |
Compared structures
- 1JF2 · Crystal Structure of W92F obelin mutant from Obelia longissima at 1.72 Angstrom resolution · 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 0.98
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 1JF2 · PDBe 1JF2 · UniProt Q27709
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