MolNFT v1 · #91516 · protein
Pylc in complex with L-lysine
4FFL: “Pylc in complex with L-lysine”. X-ray diffraction, 6 ligands (LYS, ADP, ATP), 1 pocket (best druggability 0.80). MolNFT v1 #91516 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4FFL
- Type
- protein
- Length
- 353 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pylc
- UniProt
- Q46E79
- Ligands
- LYS, ADP, ATP, MG, PO4, CO3
- Pockets
- 1 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pylc | protein | 353 | 30% helix, 32% strand | Q46E79 |
Ligands and binding sites
- LYS · Lysine · ligand · chains A
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- MG · Magnesium ion · metal · 3 copies · chains A
- PO4 · Phosphate ion · ion · chains A
- CO3 · Carbonate ion · ion · 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 | 529 | 0.80 | 0.86 | 63 | LYS, ADP, PO4, MG, CO3, ATP |
Compared structures
- 4FFL · PylC in complex with L-lysine · 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 Q46E79
- Elsewhere: RCSB PDB 4FFL · PDBe 4FFL · UniProt Q46E79
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