Research workbench
The crystal structure of a radical SAM enzyme blse involved in the biosynthesis of blasticidin S
Analyse The crystal structure of a radical SAM enzyme blse involved in the biosynthesis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7VOC
- Type
- protein
- Length
- 328 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A1B1AYF2
- Ligands
- SF4, 7QO
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | — | protein | 328 | — | A0A1B1AYF2 |
Ligands and binding sites
- SF4 · Iron/sulfur cluster · ligand · 2 copies · chains C
- 7QO · (2~{S},3~{S},4~{S},5~{R},6~{R})-6-(4-azanyl-2-oxidanylidene-pyrimidin-1-yl)-3,4,5-tris(oxidanyl) oxane-2-carboxylic acid · ligand · chains C
- GOL · Glycerol · additive · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7VOC · The crystal structure of a Radical SAM Enzyme BlsE involved in the Biosynthesis of… · the same entry in another collection · chain C against C, 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 A0A1B1AYF2
- Elsewhere: RCSB PDB 7VOC · PDBe 7VOC · UniProt A0A1B1AYF2
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