MolNFT v1 · #104202 · protein
Structure of the OSSERK2 leucine rich repeat extracellular domain
4Q3G: “Structure of the OSSERK2 leucine rich repeat extracellular domain”. X-ray diffraction, 1 ligand (NAG), 1 pocket (best druggability 0.42). MolNFT v1 #104202 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4Q3G
- Type
- protein
- Length
- 437 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- OSSERK2
- Ligands
- NAG
- Pockets
- 1 · best druggability 0.42
Structure
x-ray diffraction · 2 distinct chains · 23% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | OSSERK2 | protein | 219 | 23% helix, 17% strand | — |
| B | OSSERK2 | protein | 218 | 23% helix, 17% strand | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 164 | 0.42 | 0.73 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 636 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
- 4Q3G · Structure of the OsSERK2 leucine rich repeat extracellular domain · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 4Q3G · PDBe 4Q3G
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.