MolNFT v1 · #128787 · protein
Crystal structure of bifunctional dehydratase-cyclase domain in ambruticin biosynthesis
5O15: “Crystal structure of bifunctional dehydratase-cyclase domain in ambruticin biosynthesis”. X-ray diffraction. MolNFT v1 #128787 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5O15
- Type
- protein
- Length
- 571 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A1YBQ4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 289 | — | A1YBQ4 |
| B | — | protein | 282 | — | A1YBQ4 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5O15 · Crystal structure of bifunctional dehydratase-cyclase domain in ambruticin 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 A1YBQ4
- Elsewhere: RCSB PDB 5O15 · PDBe 5O15 · UniProt A1YBQ4
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