Research workbench
The crystal structure of acyltransferase in complex with decanoyl-CoA
Analyse The crystal structure of acyltransferase in complex with decanoyl-CoA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MFK
- Type
- protein
- Length
- 323 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative uncharacterized protein TCP24
- EC
- 2.3.1.-
- UniProt
- Q70AY4
- Ligands
- MFK, SO4
- Pockets
- 2 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative uncharacterized protein TCP24 (EC 2.3.1.-) | protein | 323 | 52% helix, 10% strand | Q70AY4 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 671 | 0.73 | 0.79 | 62 | MFK |
| 2 | 69 | 0.32 | 0.74 | 22 | empty |
Compared structures
- 4MFK · The crystal structure of acyltransferase in complex with decanoyl-CoA · 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 Q70AY4
- Elsewhere: RCSB PDB 4MFK · PDBe 4MFK · UniProt Q70AY4
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