MolNFT v1 · #152721 · protein
Green fluorescent protein variant gfpuv with the modification to 6- hydroxynorleucine at the C-terminus
6IR7: “Green fluorescent protein variant gfpuv with the modification to 6- hydroxynorleucine at the C-terminus”. X-ray diffraction, 2 ligands (CRO, SO4), 2 pockets (best druggability 0.75). MolNFT v1 #152721 on GenesisL1: 3D structure…
- PDB
- 6IR7
- Type
- protein
- Length
- 232 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Green fluorescent protein
- UniProt
- P42212
- Ligands
- CRO, SO4
- Pockets
- 2 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Green fluorescent protein | protein | 232 | 13% helix, 50% strand | P42212 |
Ligands and binding sites
- CRO · {2-[(1R,2R)-1-amino-2-hydroxypropyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid · ligand · chains A
- SO4 · Sulfate ion · ion · chains A
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 85 | 0.75 | 0.97 | 21 | CRO |
| 2 | 67 | 0.36 | 0.78 | 14 | empty |
Modifications
Observed in the structure: 2 cofactor, 1 modified (chromophore, nonstandard).
Compared structures
- 6IR7 · Green fluorescent protein variant GFPuv with the modification to 6-hydroxynorleucine at… · the same entry in another collection · chain A against A, TM-score 1.00
- P42212 · AlphaFold monomer V2.0 prediction for green fluorescent protein (P42212) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P42212
- Elsewhere: RCSB PDB 6IR7 · PDBe 6IR7 · UniProt P42212
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