Aequorea victoria
| Assembly | Physical composition | Protein state | Molecular copy count | Associated components | Data consistency |
|---|---|---|---|---|---|
| 1 | Protein monomer | Monomer | Protein 1 | water × 1 | Consistent with protein count |
| UniProt name | Q93125_AEQVI |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–236； UniProt 1–238 |
The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.
| Entry ID entry_id | 2q6p |
| Deposition date deposition_date | 2007-06-05 |
| Structure title title | The Chemical Control of Protein Folding: Engineering a Superfolder Green Fluorescent Protein |
| Keywords keywords | GFP, Noncanonical amino acid, superfolder, LUMINESCENT PROTEIN; LUMINESCENT PROTEIN |
| Experimental Method method | X-RAY DIFFRACTION |
This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.
Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)
| Rg（Guinier） | 18.14 Å |
| Rg (electron density) | 16.83 Å |
| Total Rg | 17.86 Å |
| Atom count | 1806 |
| Residues | 213 |
| Excluded volume | 31965 ų |
| Maximum q | 0.500 Å⁻¹ |
| Domain ID domain_id | d2q6pa_ |
| Class class | d — Alpha and beta proteins (a+b) |
| Fold Fold fold | d.22 — GFP-like |
| Superfamily Superfamily superfamily | d.22.1 — GFP-like |
| Family Family family | d.22.1.1 — Fluorescent proteins |
| Domain ID domain_id | 2q6pA00 |
| Class class | 2 — Mainly Beta |
| Architecture architecture | 40 — Beta Barrel |
| Topology topology | 155 — Green Fluorescent Protein |
| Homologous superfamily homologous superfamily | 10 — Green fluorescent protein |