MolNFT v1 · #34894 · protein
Crystal structure of a green fluorescent protein variant S65T/H148D at pH 10
2DUE: “Crystal structure of a green fluorescent protein variant S65T/H148D at pH 10”. X-ray diffraction, 1 ligand (C12), 1 pocket (best druggability 0.71). MolNFT v1 #34894 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2DUE
- Type
- protein
- Length
- 219 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Green fluorescent protein
- UniProt
- P42212
- Ligands
- C12
- Pockets
- 1 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Green fluorescent protein | protein | 219 | 12% helix, 51% strand | P42212 |
Ligands and binding sites
- C12 · 2-(1-amino-2-hydroxypropyl)-4-(4-hydroxybenzyl)-1-(2-oxoethyl)-1H-imidazol-5-olate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 152 | 0.71 | 0.90 | 30 | C12 |
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 2DUE · crystal structure of a green fluorescent protein variant S65T/H148D at pH 10 · 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 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 P42212
- Elsewhere: RCSB PDB 2DUE · PDBe 2DUE · UniProt P42212
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