MolNFT v1 · #148038 · protein
Crystal structure of E282Q a. niger FDC1 with prfmn in the hydroxylated form
6EV5: “Crystal structure of E282Q a. niger FDC1 with prfmn in the hydroxylated form”. X-ray diffraction, 4 ligands (BYN, K, MN). MolNFT v1 #148038 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6EV5
- Type
- protein
- Length
- 500 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A2QHE5
- Ligands
- BYN, K, MN, SCN
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 500 | — | 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.
Compared structures
- 6EV5 · Crystal structure of E282Q 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 6EV5 · PDBe 6EV5 · UniProt A2QHE5
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