Research workbench
Crystal structure of the acyltransferase domain of the iterative polyketide synthase in enediyne biosynthesis reveals the molecular basis of substrate specificity
Analyse Crystal structure of the acyltransferase domain of the iterative polyketide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AMO
- Type
- protein
- Length
- 371 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DYNE8
- UniProt
- Q84HI8
- Pockets
- 3 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DYNE8 | protein | 371 | 46% helix, 18% strand | Q84HI8 |
Ligands and binding sites
- ACY · Acetic acid · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 258 | 0.68 | 0.83 | 37 | ACY |
| 2 | 130 | 0.39 | 0.74 | 29 | empty |
| 3 | 67 | 0.27 | 0.72 | 19 | empty |
Compared structures
- 4AMO · Crystal Structure of the Acyltransferase Domain of the Iterative Polyketide Synthase in… · 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 Q84HI8
- Elsewhere: RCSB PDB 4AMO · PDBe 4AMO · UniProt Q84HI8
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