Research workbench
Atomic resolution structure of obelin from obelia longissima
Analyse Atomic resolution structure of obelin from obelia longissima in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QV1
- Type
- protein
- Length
- 187 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Obelin
- EC
- 1.13.12.5
- UniProt
- Q27709
- Ligands
- CZH, CO, CA, K
- Pockets
- 1 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 62% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Obelin (EC 1.13.12.5) | protein | 187 | 62% helix, 3% strand | Q27709 |
Ligands and binding sites
- CZH · C2-hydroperoxy-coelenterazine · ligand · chains A
- CO · Cobalt (II) ion · metal · 2 copies · chains A
- CA · Calcium ion · metal · chains A
- K · Potassium ion · metal · chains A
- GOL · Glycerol · additive · 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 | 203 | 0.84 | 0.97 | 33 | CZH |
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 Q27709
- Elsewhere: RCSB PDB 1QV1 · PDBe 1QV1 · UniProt Q27709
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