Research workbench
Structure of E. faecalis fabh in complex with acetyl CoA
Analyse Structure of E. faecalis fabh in complex with acetyl CoA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3IL4
- Type
- protein
- Length
- 1,270 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-oxoacyl-[acyl-carrier-protein] synthase 3
- EC
- 2.3.1.180
- UniProt
- Q820T1
- Ligands
- ACO
- Pockets
- 11 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | 3-oxoacyl-[acyl-carrier-protein] synthase 3 (EC 2.3.1.180) | protein | 318 | 40% helix, 26% strand | Q820T1 |
| B, C | 3-oxoacyl-[acyl-carrier-protein] synthase 3 (EC 2.3.1.180) | protein | 317 | 39% helix, 26% strand | Q820T1 |
Ligands and binding sites
- ACO · Acetyl coenzyme *A · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 79 | 0.75 | 0.98 | 19 | empty |
| 2 | 219 | 0.72 | 0.88 | 35 | empty |
| 3 | 247 | 0.66 | 0.83 | 34 | empty |
| 4 | 191 | 0.65 | 0.84 | 27 | ACO |
| 5 | 221 | 0.64 | 0.82 | 31 | ACO |
Interfaces
3 interfaces between chains.
- C–D · 3279 Ų buried · 33 hydrogen bonds · protein-protein
- A–B · 3271 Ų buried · 37 hydrogen bonds · protein-protein
- A–D · 716 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (oxidation).
Compared structures
- 3IL4 · Structure of E. faecalis FabH in complex with acetyl CoA · the same entry in another collection · chain D against D, TM-score 1.00
- Q820T1 · AlphaFold monomer V2.0 prediction for 3-oxoacyl-[acyl-carrier- protein] synthase 3… · a predicted model of the same protein · chain C 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 Q820T1
- Elsewhere: RCSB PDB 3IL4 · PDBe 3IL4 · UniProt Q820T1
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