Research workbench
Crystal structure of Green Fluorescent Protein (GFP); S65T, Y66(2,3-F2Y), H148D; circular permutant (50-51)
Analyse Crystal structure of Green Fluorescent Protein (GFP); S65T, Y66(2,3-F2Y)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6OGC
- Type
- protein
- Length
- 460 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.178
- Source
- Aequorea victoria
- Molecule
- Crystal structure of Green Fluorescent Protein (GFP); S65T, Y66(2,3-F2Y), H148D; circular…
- Pockets
- 6 · best druggability 0.77
Structure
x-ray diffraction · resolution 1.178 · 2 distinct chains · 10% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Crystal structure of Green Fluorescent Protein (GFP); S65T, Y66(2,3-F2Y), H148D; circular permutant (50-51) | protein | 233 | 11% helix, 50% strand | — |
| A | Crystal structure of Green Fluorescent Protein (GFP); S65T, Y66(2,3-F2Y), H148D; circular permutant (50-51) | protein | 227 | 9% helix, 51% strand | — |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 101 | 0.77 | 0.97 | 26 | empty |
| 2 | 94 | 0.77 | 0.98 | 24 | empty |
| 3 | 206 | 0.50 | 0.76 | 34 | empty |
| 4 | 220 | 0.49 | 0.75 | 35 | empty |
| 5 | 62 | 0.29 | 0.74 | 18 | empty |
Interfaces
1 interface between chains.
- B–A · 670 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 6OGC · Crystal structure of green fluorescent protein (GFP); S65T, Y66(2,3- F2Y), H148D… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 6OGC · PDBe 6OGC
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