MolNFT v1 · #105916 · protein
Structure of a plant specific C2 domain protein, OSGAP1 from rice
4RJ9 · C2 domain-containing protein-like: “Structure of a plant specific C2 domain protein, OSGAP1 from rice”. X-ray diffraction, 1 ligand (K), 1 pocket (best druggability 0.39). MolNFT v1 #105916 on GenesisL1: 3D structure, binding sites…
- PDB
- 4RJ9
- Type
- protein
- Length
- 161 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- C2 domain-containing protein-like
- EC
- 6.5.1.1
- UniProt
- Q6YWF1
- Ligands
- K
- Pockets
- 1 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | C2 domain-containing protein-like (EC 6.5.1.1) | protein | 161 | 4% helix, 48% strand | Q6YWF1 |
Ligands and binding sites
- K · Potassium ion · metal · 2 copies · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 57 | 0.39 | 0.80 | 18 | empty |
Compared structures
- 4RJ9 · Structure of a plant specific C2 domain protein, OsGAP1 from rice · the same entry in another collection · chain A against A, TM-score 1.00
- Q6YWF1 · AlphaFold monomer V2.0 prediction for GTPase activating protein 1 (Q6YWF1) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q6YWF1
- Elsewhere: RCSB PDB 4RJ9 · PDBe 4RJ9 · UniProt Q6YWF1
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.