MolNFT v1 · #162237 · protein
Aspergillus niger ferulic acid decarboxylase (fdc) L439G variant in complex with the covalent adduct formed between prfmn cofactor and phenylpropiolic acid (INT1')
6R30: “Aspergillus niger ferulic acid decarboxylase (fdc) L439G variant in complex with the covalent adduct formed…”. X-ray diffraction, 4 ligands (JQZ, JQ8, K). MolNFT v1 #162237 on GenesisL1: 3D structure, binding sites and pockets in…
- 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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