MolNFT v1 · #91521 · protein
Semet-labeled pylc (remote)
4FFR: “Semet-labeled pylc (remote)”. X-ray diffraction, 2 ligands (ATP, MG), 1 pocket (best druggability 0.80). MolNFT v1 #91521 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4FFR
- Type
- protein
- Length
- 347 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pylc
- UniProt
- Q46E79
- Ligands
- ATP, MG
- Pockets
- 1 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pylc | protein | 347 | 29% helix, 32% strand | Q46E79 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A
- MG · Magnesium ion · metal · 4 copies · 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 | 541 | 0.80 | 0.86 | 65 | ATP, MG |
Modifications
Observed in the structure: 7 modified (engineered).
Compared structures
- 4FFR · SeMet-labeled PylC (remote) · 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 4FFR · PDBe 4FFR · UniProt Q46E79
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.