Research workbench
Probing the role of tryptophans in aequorea victoria green fluorescent proteins with an expanded genetic code
Analyse Probing the role of tryptophans in aequorea victoria green fluorescent proteins… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- 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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