Research workbench
Cryo-EM structure of the elongation module of the bacillamide nrps, bmdb, in complex with the oxidase, bmdc
Analyse Cryo-EM structure of the elongation module of the bacillamide nrps, bmdb, in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LY4
- Type
- protein
- Length
- 1,474 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Ligands
- FMN
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | — | protein | 323 | — | — |
| E | — | protein | 828 | — | — |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 2 copies · chains A, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7LY4 · Cryo-EM structure of the elongation module of the bacillamide NRPS, BmdB, in complex with… · 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
- Elsewhere: RCSB PDB 7LY4 · PDBe 7LY4
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