Eleven strands make a can. One helix runs up the middle, and three of its residues turn themselves into a dye. Nothing is added: the protein builds its own chromophore and then holds it still.
—
| fold | — |
| span | — |
| modelled | — |
| completeness | — |
| helix / strand | — |
| chromophore | — |
| made from | — |
| substitutions declared | — |
| phenol O to Thr203 | — |
| phenol O to His148 | — |
| Glu222 to Ser205 | — |
| biological unit | — |
| brought by the crystal | — |
| extents Å | — |
| frame | — |
—
—
Both are fluorescent and both are engineered: each carries Q80R, so neither is strictly the wild-type protein. What changes the colour is the made from row, read off the atoms rather than off the sequence records — Y66H sits inside the fused chromophore residue, where SEQADV does not report it.
The blue variant is superposed on 1GFL by its α-carbons, so flipping between them moves only what actually moved. Both are the same protein under the same numbering.
Ribbon colour is secondary structure, the repo default. The ball-and-stick inside is the chromophore and the five side chains around it — Arg96 and Glu222 below, His148, Thr203 and Ser205 on the phenol end. Chain A's, in both views.
Turn the molecule, click copy, then paste into
view.basis in proteins.js with
by: 'human'.