Research workbench
Ferredoxin reductase in carbazole 1,9A-dioxygenase (FAD apo form)
Analyse Ferredoxin reductase in carbazole 1,9A-dioxygenase (FAD apo form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7C3B
- Type
- protein
- Length
- 964 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q84II0
- Ligands
- FES, NI, CL, IOD
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 324 | — | Q84II0 |
| B | — | protein | 306 | — | Q84II0 |
| C | — | protein | 334 | — | Q84II0 |
Ligands and binding sites
- FES · Fe2/s2 (inorganic) cluster · ligand · 3 copies · chains A, B, C
- NI · Nickel (II) ion · metal · chains A, B, C
- CL · Chloride ion · ion · 18 copies · chains A, B, C
- IOD · Iodide ion · ion · 3 copies · chains A, B, C
- ACT · Acetate ion · additive · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7C3B · Ferredoxin reductase in carbazole 1,9a-dioxygenase (FAD apo form) · 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 Q84II0
- Elsewhere: RCSB PDB 7C3B · PDBe 7C3B · UniProt Q84II0
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