MolNFT v1 · #171603 · protein
Room temperature xfel isopenicillin N synthase structure in complex with fe and acv after exposure to dioxygen for 500MS without glycerol.
6ZAL: “Room temperature xfel isopenicillin N synthase structure in complex with fe and acv after exposure to…”. X-ray diffraction, 4 ligands (ACV, FE2, SO4). MolNFT v1 #171603 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6ZAL
- Type
- protein
- Length
- 329 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P05326
- Ligands
- ACV, FE2, SO4, OXY
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
- FE2 · Fe (II) ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
- OXY · Oxygen molecule · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6ZAL · Room temperature XFEL Isopenicillin N synthase structure in complex with Fe and ACV after… · 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 6ZAL · PDBe 6ZAL · UniProt P05326
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