MolNFT v1 · #37391 · protein
Reduced enolate chromophore intermediate for GFP variant
2FZU · Green fluorescent protein: “Reduced enolate chromophore intermediate for GFP variant”. X-ray diffraction, 2 ligands (C12, MG), 2 pockets (best druggability 0.76). MolNFT v1 #37391 on GenesisL1: 3D structure, binding sites and…
- PDB
- 2FZU
- Type
- protein
- Length
- 233 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Green fluorescent protein
- UniProt
- P42212
- Ligands
- C12, MG
- Pockets
- 2 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 14% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Green fluorescent protein | protein | 233 | 14% helix, 50% strand | P42212 |
Ligands and binding sites
- C12 · 2-(1-amino-2-hydroxypropyl)-4-(4-hydroxybenzyl)-1-(2-oxoethyl)-1H-imidazol-5-olate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- EDO · 1,2-ethanediol · additive · 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 | 84 | 0.76 | 0.98 | 25 | C12 |
| 2 | 86 | 0.39 | 0.77 | 19 | empty |
Modifications
Observed in the structure: 2 covalent (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 P42212
- Elsewhere: RCSB PDB 2FZU · PDBe 2FZU · UniProt P42212
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