Research workbench
Fluorescent protein ASFP595, A143S, on-state, 1MIN irradiation
Analyse Fluorescent protein ASFP595, A143S, on-state, 1MIN irradiation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2A54
- Type
- protein
- Length
- 457 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GFP-like non-fluorescent chromoprotein FP595 chain 1; GFP-like non-fluorescent…
- UniProt
- Q9GZ28
- Ligands
- NRQ, CL
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · 3 distinct chains · 8% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GFP-like non-fluorescent chromoprotein FP595 chain 1 | protein | 64 | 16% helix, 52% strand | Q9GZ28 |
| B, D | GFP-like non-fluorescent chromoprotein FP595 chain 2 | protein | 167 | 4% helix, 54% strand | Q9GZ28 |
| C | GFP-like non-fluorescent chromoprotein FP595 chain 1 | protein | 59 | 12% helix, 56% strand | Q9GZ28 |
Ligands and binding sites
- NRQ · {(4Z)-4-(4-hydroxybenzylidene)-2-[3-(methylthio) propanimidoyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid · ligand · 2 copies · chains A, B, C, D
- CL · Chloride ion · ion · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 82 | 0.76 | 0.99 | 24 | NRQ |
| 2 | 77 | 0.75 | 0.98 | 26 | NRQ |
| 3 | 93 | 0.46 | 0.81 | 15 | empty |
| 4 | 64 | 0.32 | 0.75 | 20 | empty |
Interfaces
5 interfaces between chains.
- C–D · 2162 Ų buried · 37 hydrogen bonds · protein-protein
- A–B · 2039 Ų buried · 38 hydrogen bonds · protein-protein
- B–D · 795 Ų buried · 15 hydrogen bonds · protein-protein
- B–C · 169 Ų buried · 3 hydrogen bonds · protein-protein
- A–D · 153 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 cofactor (chromophore).
Compared structures
- 2A54 · fluorescent protein asFP595, A143S, on-state, 1min irradiation · the same entry in another collection · chain D against D, TM-score 1.00
- Q9GZ28 · AlphaFold monomer V2.0 prediction for GFP-like non-fluorescent chromoprotein FP595… · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q9GZ28
- Elsewhere: RCSB PDB 2A54 · PDBe 2A54 · UniProt Q9GZ28
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