2Q6P
The Chemical Control of Protein Folding: Engineering a Superfolder Green Fluorescent Protein
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A (A) | Green fluorescent protein mutant 3 | polymer | 238 | 27091.3 | 1 | UniProt (Q93125) Pfam (PF01353) UniProt (by SIFTS) (P42212) | Aequorea victoria | |
2 | B (A) | water | water | 18.0 | 117 | Chemie (HOH) |
Sequence modifications
A: 1 - 238 (UniProt: Q93125)
PDB | External Database | Details |
---|---|---|
4fb 13 | Pro 13 | modified residue |
4fb 54 | Pro 54 | modified residue |
4fb 56 | Pro 56 | modified residue |
4fb 58 | Pro 58 | modified residue |
Leu 64 | Phe 64 | engineered mutation |
Cro 66 | Gly 65 | chromophore |
Cro 66 | Tyr 66 | chromophore |
Cro 66 | Gly 67 | chromophore |
Ser 72 | Ala 72 | engineered mutation |
4fb 75 | Pro 75 | modified residue |
Arg 80 | Gln 80 | engineered mutation |
4fb 89 | Pro 89 | modified residue |
4fb 187 | Pro 187 | modified residue |
4fb 192 | Pro 192 | modified residue |
4fb 196 | Pro 196 | modified residue |
4fb 211 | Pro 211 | modified residue |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 1 |
Total formula weight | 27091.3 | |
All* | Total formula weight | 27091.3 |