Research workbench
Structure of beta-ketoacetyl-CoA reductase (fabg) from staphylococcus aureus complex with NADPH
Analyse Structure of beta-ketoacetyl-CoA reductase (fabg) from staphylococcus aureus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SJ7
- Type
- protein
- Length
- 482 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-oxoacyl-(acyl-carrier-protein) reductase
- EC
- 1.1.1.100
- UniProt
- Q2FZ53
- Ligands
- NDP
- Pockets
- 4 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-oxoacyl-(acyl-carrier-protein) reductase (EC 1.1.1.100) | protein | 239 | 48% helix, 17% strand | Q2FZ53 |
| B | 3-oxoacyl-(acyl-carrier-protein) reductase (EC 1.1.1.100) | protein | 243 | 51% helix, 16% strand | Q2FZ53 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- PG4 · Tetraethylene glycol · additive · 3 copies · chains A, B
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 | 524 | 0.67 | 0.78 | 45 | NDP, PG4 |
| 2 | 473 | 0.64 | 0.77 | 47 | NDP, PG4 |
| 3 | 143 | 0.47 | 0.78 | 22 | empty |
| 4 | 54 | 0.35 | 0.79 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1635 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 3SJ7 · Structure of beta-ketoacetyl-CoA reductase (FabG) from Staphylococcus aureus complex with… · 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 Q2FZ53
- Elsewhere: RCSB PDB 3SJ7 · PDBe 3SJ7 · UniProt Q2FZ53
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.