Research workbench
Aspergillus niger ferulic acid decarboxylase (fdc) L439G variant in complex with the covalent adduct formed between prfmn cofactor and phenylpropiolic acid (INT1')
Analyse Aspergillus niger ferulic acid decarboxylase (fdc) L439G variant in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6R30
- Type
- protein
- Length
- 500 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A3F3RNU4
- Ligands
- JQZ, JQ8, K, MN
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 500 | — | A0A3F3RNU4 |
Ligands and binding sites
- JQZ · prFMN cofactor and phenylpropiolic acid · ligand · chains A
- JQ8 · phenylpropiolic 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.
Compared structures
- 6R30 · Aspergillus niger ferulic acid decarboxylase (Fdc) L439G variant in complex with the… · 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 A0A3F3RNU4
- Elsewhere: RCSB PDB 6R30 · PDBe 6R30 · UniProt A0A3F3RNU4
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