MolNFT v1 · #30612 · protein
Crystal structure of AMFP486 E150Q
2A48 · GFP-like fluorescent chromoprotein AMFP486: “Crystal structure of AMFP486 E150Q”. X-ray diffraction, 1 ligand (CR7), 1 pocket (best druggability 0.76). MolNFT v1 #30612 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2A48
- Type
- protein
- Length
- 212 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GFP-like fluorescent chromoprotein AMFP486
- UniProt
- Q9U6Y6
- Ligands
- CR7
- Pockets
- 1 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 58% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GFP-like fluorescent chromoprotein AMFP486 | protein | 212 | 4% helix, 58% strand | Q9U6Y6 |
Ligands and binding sites
- CR7 · [(4Z)-2-[(1S)-1,5-diaminopentyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid · ligand · chains A
- BME · Beta-mercaptoethanol · additive · 3 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 106 | 0.76 | 0.97 | 30 | CR7 |
Modifications
Observed in the structure: 5 covalent (additive adduct, covalent ligand).
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 Q9U6Y6
- Elsewhere: RCSB PDB 2A48 · PDBe 2A48 · UniProt Q9U6Y6
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