Research workbench
Structure of the fluorescent protein ASFP499 from anemonia sulcata
Analyse Structure of the fluorescent protein ASFP499 from anemonia sulcata in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2C9I
- Type
- protein
- Length
- 1,797 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Green fluorescent protein ASFP499
- UniProt
- Q9GPI6
- Ligands
- CRQ
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 4% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D, E, G | Green fluorescent protein ASFP499 | protein | 225 | 4% helix, 54% strand | Q9GPI6 |
| B, F, H | Green fluorescent protein ASFP499 | protein | 224 | 4% helix, 54% strand | Q9GPI6 |
Ligands and binding sites
- CRQ · [2-(3-carbamoyl-1-imino-propyl)-4-(4-hydroxy-benzylidene)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid · ligand · 8 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1188 | 0.85 | 0.86 | 114 | empty |
| 2 | 669 | 0.84 | 0.88 | 73 | empty |
| 3 | 90 | 0.77 | 0.98 | 28 | CRQ |
| 4 | 87 | 0.77 | 0.99 | 28 | CRQ |
| 5 | 90 | 0.76 | 0.98 | 26 | CRQ |
Interfaces
15 interfaces between chains.
- A–B · 1875 Ų buried · 24 hydrogen bonds · protein-protein
- E–F · 1839 Ų buried · 26 hydrogen bonds · protein-protein
- C–D · 1819 Ų buried · 21 hydrogen bonds · protein-protein
- G–H · 1794 Ų buried · 26 hydrogen bonds · protein-protein
- F–G · 1055 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 11 cofactor (chromophore).
Compared structures
- 2C9I · Structure of the fluorescent protein asFP499 from Anemonia sulcata · 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
- Every structure of UniProt Q9GPI6
- Elsewhere: RCSB PDB 2C9I · PDBe 2C9I · UniProt Q9GPI6
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