Research workbench
O2-, plp-dependent desaturase PLU4 holo-enzyme
Analyse O2-, plp-dependent desaturase PLU4 holo-enzyme in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7N79
- Type
- protein
- Length
- 756 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- AMINOTRAN_1_2 domain-containing protein
- UniProt
- A0A0C1MLE8
- Pockets
- 9 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | AMINOTRAN_1_2 domain-containing protein | protein | 378 | 51% helix, 13% strand | A0A0C1MLE8 |
Ligands and binding sites
- ACT · Acetate ion · additive · 3 copies · chains A, B
- 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.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 74 | 0.74 | 0.98 | 22 | EDO |
| 2 | 202 | 0.62 | 0.83 | 28 | ACT, EDO |
| 3 | 177 | 0.58 | 0.82 | 21 | empty |
| 4 | 52 | 0.54 | 0.90 | 18 | empty |
| 5 | 91 | 0.48 | 0.81 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 2394 Ų buried · 26 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (cofactor).
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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