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The structure of the bifunctional ACETYLTRANSFERASE/DECARBOXYLASE lnmk from the leinamycin biosynthetic pathway revealing novel activity for a double hot dog fold
Analyse The structure of the bifunctional ACETYLTRANSFERASE/DECARBOXYLASE lnmk from the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HZN
- Type
- protein
- Length
- 299 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional methylmalonyl-COA:ACP ACYLTRANSFERASE/DECARBOXYLASE
- UniProt
- Q8GGP1
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional methylmalonyl-COA:ACP ACYLTRANSFERASE/DECARBOXYLASE | protein | 299 | 23% helix, 35% strand | Q8GGP1 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 167 | 0.69 | 0.88 | 24 | empty |
| 2 | 172 | 0.62 | 0.83 | 27 | GOL |
| 3 | 55 | 0.26 | 0.73 | 13 | empty |
| 4 | 51 | 0.25 | 0.73 | 18 | empty |
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 4HZN · The Structure of the Bifunctional Acetyltransferase/Decarboxylase LnmK from the… · 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 Q8GGP1
- Elsewhere: RCSB PDB 4HZN · PDBe 4HZN · UniProt Q8GGP1
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