Research workbench
Structure of non-heme iron enzyme tropc: radical tropolone biosynthesis
Analyse Structure of non-heme iron enzyme tropc: radical tropolone biosynthesis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XJJ
- Type
- protein
- Length
- 291 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- B8M9K5
- Ligands
- FE, YT3
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 291 | — | B8M9K5 |
Ligands and binding sites
- FE · Fe (III) ion · metal · chains A
- YT3 · Yttrium (III) ion · metal · chains A
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6XJJ · Structure of non-heme iron enzyme TropC: Radical tropolone biosynthesis · the same entry in another collection · chain A against A, TM-score 1.00
- B8M9K5 · AlphaFold monomer V2.0 prediction for 2-oxoglutarate-dependent dioxygenase tropc (B8M9K5) · 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 B8M9K5
- Elsewhere: RCSB PDB 6XJJ · PDBe 6XJJ · UniProt B8M9K5
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