Research workbench
R52Q mutant of photoactive yellow protein, P65 form
Analyse R52Q mutant of photoactive yellow protein, P65 form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2D02
- Type
- protein
- Length
- 125 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Photoactive yellow protein
- UniProt
- P16113
- Ligands
- HC4
- Pockets
- 1 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Photoactive yellow protein | protein | 125 | 34% helix, 28% strand | P16113 |
Ligands and binding sites
- HC4 · 4'-hydroxycinnamic acid · 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 | 56 | 0.52 | 0.87 | 18 | HC4 |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 2D02 · R52Q Mutant of Photoactive Yellow Protein, P65 Form · 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 P16113
- Elsewhere: RCSB PDB 2D02 · PDBe 2D02 · UniProt P16113
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.