MolNFT v1 · #148041 · protein
Structure of E277Q a. niger FDC1 with prfmn in the hydroxylated form
6EV8 · Ferulic acid decarboxylase 1: “Structure of E277Q a. niger FDC1 with prfmn in the hydroxylated form”. X-ray diffraction, 4 ligands (BYN, K, MN), 4 pockets (best druggability 0.85). MolNFT v1 #148041 on GenesisL1: 3D structure…
- PDB
- 6EV8
- Type
- protein
- Length
- 500 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferulic acid decarboxylase 1
- EC
- 4.1.1.102
- UniProt
- A2QHE5
- Ligands
- BYN, K, MN, SCN
- Pockets
- 4 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferulic acid decarboxylase 1 (EC 4.1.1.102) | protein | 500 | 31% helix, 23% strand | A2QHE5 |
Ligands and binding sites
- BYN · hydroxylated prenyl-FMN · ligand · chains A
- K · Potassium ion · metal · 2 copies · chains A
- MN · Manganese (II) ion · metal · chains A
- SCN · Thiocyanate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 333 | 0.85 | 0.95 | 38 | K, BYN, SCN |
| 2 | 259 | 0.61 | 0.80 | 42 | empty |
| 3 | 53 | 0.31 | 0.76 | 13 | empty |
| 4 | 70 | 0.29 | 0.73 | 24 | empty |
Compared structures
- 6EV8 · Structure of E277Q A. niger Fdc1 with prFMN in the hydroxylated form · the same entry in another collection · chain A against A, TM-score 1.00
- A2QHE5 · AlphaFold monomer V2.0 prediction for ferulic acid decarboxylase 1 (A2QHE5) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 A2QHE5
- Elsewhere: RCSB PDB 6EV8 · PDBe 6EV8 · UniProt A2QHE5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.