Research workbench
Structure of a. niger fdc T395M R435P P438W variant (anfdcii) in complex with prfmn
Analyse Structure of a. niger fdc T395M R435P P438W variant (anfdcii) in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7NF4
- Type
- protein
- Length
- 999 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A2QHE5
- Ligands
- BYN, K, MN
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 504 | — | A2QHE5 |
| B | — | protein | 495 | — | A2QHE5 |
Ligands and binding sites
- BYN · hydroxylated prenyl-FMN · ligand · 2 copies · chains A, B
- K · Potassium ion · metal · 5 copies · chains A, B
- MN · Manganese (II) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7NF4 · Structure of A. niger Fdc T395M R435P P438W variant (AnFdcII) in complex with prFMN · 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 B 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 A2QHE5
- Elsewhere: RCSB PDB 7NF4 · PDBe 7NF4 · UniProt A2QHE5
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