Research workbench
Aspergillus niger ferulic acid decarboxylase (fdc) in complex with FMN and cinnamic acid
Analyse Aspergillus niger ferulic acid decarboxylase (fdc) in complex with FMN and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6R2P
- Type
- protein
- Length
- 497 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
- FMN, TCA, K, MN
- Pockets
- 3 · 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 | 497 | 31% helix, 23% strand | A2QHE5 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · chains A
- TCA · Phenylethylenecarboxylic acid · ligand · chains A
- K · Potassium ion · metal · 2 copies · chains A
- MN · Manganese (II) ion · metal · 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 | 324 | 0.85 | 0.95 | 40 | FMN, K, TCA |
| 2 | 236 | 0.56 | 0.78 | 41 | empty |
| 3 | 52 | 0.31 | 0.76 | 14 | empty |
Compared structures
- 6R2P · Aspergillus niger ferulic acid decarboxylase (Fdc) in complex with FMN and cinnamic acid · 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 6R2P · PDBe 6R2P · UniProt A2QHE5
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