MolNFT v1 · #182877 · protein
O2-, plp-dependent desaturase PLU4 holo-enzyme
7N79: “O2-, plp-dependent desaturase PLU4 holo-enzyme”. X-ray diffraction. MolNFT v1 #182877 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7N79
- Type
- protein
- Length
- 756 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A0C1MLE8
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 378 | — | A0A0C1MLE8 |
Ligands and binding sites
- ACT · Acetate ion · additive · 3 copies · chains A
- EDO · 1,2-ethanediol · additive · 3 copies · chains A, B
- BTB · 2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7N79 · O2-, PLP-dependent desaturase Plu4 holo-enzyme · 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 A0A0C1MLE8
- Elsewhere: RCSB PDB 7N79 · PDBe 7N79 · UniProt A0A0C1MLE8
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