MolNFT v1 · #170224 · protein
Isopenicillin N synthase in complex with acv and fe under anaerobic environment using ft-ssx methods
6Y0O: “Isopenicillin N synthase in complex with acv and fe under anaerobic environment using ft-ssx methods”. X-ray diffraction, 3 ligands (ACV, FE, SO4). MolNFT v1 #170224 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6Y0O
- Type
- protein
- Length
- 329 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P05326
- Ligands
- ACV, FE, SO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 329 | — | P05326 |
Ligands and binding sites
- ACV · L-D-(A-aminoadipoyl)-L-cysteinyl-D-valine · ligand · chains A
- FE · Fe (III) ion · metal · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6Y0O · isopenicillin N synthase in complex with ACV and Fe under anaerobic environment using… · the same entry in another collection · chain A against A, TM-score 1.00
- P05326 · AlphaFold monomer V2.0 prediction for isopenicillin N synthase (P05326) · 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 P05326
- Elsewhere: RCSB PDB 6Y0O · PDBe 6Y0O · UniProt P05326
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.