MolNFT v1 · #20679 · protein
Probing the role of tryptophans in aequorea victoria green fluorescent proteins with an expanded genetic code
1RM9 · Avermectin-sensitive chloride channel glucl BETA/CYAN…: “Probing the role of tryptophans in aequorea victoria green fluorescent proteins with an expanded genetic code”. X-ray diffraction, 1 ligand (4F3), 2 pockets (best druggability…
- PDB
- 1RM9
- Type
- protein
- Length
- 224 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Avermectin-sensitive chloride channel glucl BETA/CYAN fluorescent protein fusion
- UniProt
- P42212
- Ligands
- 4F3
- Pockets
- 2 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Avermectin-sensitive chloride channel glucl BETA/CYAN fluorescent protein fusion | protein | 224 | 11% helix, 54% strand | P42212 |
Ligands and binding sites
- 4F3 · [2-(1-amino-2-hydroxy-propyl)-4-(4-fluoro-1H-indol-3-ylmethyl)-5-hydroxy-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 | 91 | 0.77 | 0.98 | 26 | 4F3 |
| 2 | 73 | 0.40 | 0.79 | 15 | empty |
Modifications
Observed in the structure: 2 covalent, 1 modified (covalent ligand, nonstandard).
Compared structures
- 1RM9 · Probing the Role of Tryptophans in Aequorea Victoria Green Fluorescent Proteins with an… · the same entry in another collection · chain A against A, TM-score 1.00
- P42212 · AlphaFold monomer V2.0 prediction for green fluorescent protein (P42212) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 1RM9 · PDBe 1RM9 · UniProt P42212
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