Research workbench
Pyridine synthase, tbtd, from thiomuracin biosynthesis
Analyse Pyridine synthase, tbtd, from thiomuracin biosynthesis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WA3
- Type
- protein
- Length
- 616 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- D6Y504
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 310 | — | D6Y504 |
| B | — | protein | 306 | — | D6Y504 |
Compared structures
- 5WA3 · Pyridine synthase, TbtD, from thiomuracin biosynthesis · 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 D6Y504
- Elsewhere: RCSB PDB 5WA3 · PDBe 5WA3 · UniProt D6Y504
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