MolNFT v1 · #5579 · protein
Green fluorescent protein from aequorea victoria
1EMA: “Green fluorescent protein from aequorea victoria”. X-ray diffraction, 1 ligand (CRO), 2 pockets (best druggability 0.78). MolNFT v1 #5579 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1EMA
- Type
- protein
- Length
- 225 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Green fluorescent protein
- UniProt
- P42212
- Ligands
- CRO
- Pockets
- 2 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Green fluorescent protein | protein | 225 | 10% helix, 52% strand | P42212 |
Ligands and binding sites
- CRO · {2-[(1R,2R)-1-amino-2-hydroxypropyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 111 | 0.78 | 0.97 | 27 | CRO |
| 2 | 51 | 0.34 | 0.79 | 14 | empty |
Modifications
Observed in the structure: 4 modified, 2 cofactor (engineered, chromophore).
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 P42212
- Elsewhere: RCSB PDB 1EMA · PDBe 1EMA · UniProt P42212
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.