Research workbench
Piga with FAD and proline
Analyse Piga with FAD and proline in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6AF6
- Type
- protein
- Length
- 385 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-prolyl-[peptidyl-carrier protein] dehydrogenase
- EC
- 1.3.8.14
- UniProt
- Q5W271
- Ligands
- O4B, FAD, CL
- Pockets
- 3 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-prolyl-[peptidyl-carrier protein] dehydrogenase (EC 1.3.8.14) | protein | 385 | 57% helix, 15% strand | Q5W271 |
Ligands and binding sites
- O4B · 1,4,7,10,13,16-hexaoxacyclooctadecane · ligand · 2 copies · chains A
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 240 | 0.74 | 0.88 | 37 | FAD |
| 2 | 214 | 0.66 | 0.84 | 33 | empty |
| 3 | 104 | 0.37 | 0.74 | 15 | empty |
Compared structures
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 Q5W271
- Elsewhere: RCSB PDB 6AF6 · PDBe 6AF6 · UniProt Q5W271
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.