Research workbench
Crystal structure of the staphylococcus aureus enoyl-acyl carrier protein reductase (fabi) in complex with NADP and triclosan
Analyse Crystal structure of the staphylococcus aureus enoyl-acyl carrier protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3GR6
- Type
- protein
- Length
- 1,029 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enoyl-[acyl-carrier-protein] reductase [NADH]
- EC
- 1.3.1.9
- UniProt
- Q6GI75
- Ligands
- NAP, TCL
- Pockets
- 14 · best druggability 0.84
Structure
x-ray diffraction · 3 distinct chains · 47% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 255 | 48% helix, 15% strand | Q6GI75 |
| D, J | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 260 | 46% helix, 15% strand | Q6GI75 |
| G | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 254 | 48% helix, 15% strand | Q6GI75 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 4 copies · chains A, D, G, J
- TCL · Triclosan · ligand · 4 copies · chains A, D, G, J
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1178 | 0.84 | 0.85 | 66 | empty |
| 2 | 643 | 0.82 | 0.86 | 71 | NAP, TCL |
| 3 | 514 | 0.82 | 0.88 | 47 | NAP, TCL |
| 4 | 513 | 0.82 | 0.88 | 44 | NAP, TCL |
| 5 | 564 | 0.79 | 0.85 | 57 | NAP, TCL |
Interfaces
6 interfaces between chains.
- A–D · 1759 Ų buried · 41 hydrogen bonds · protein-protein
- G–J · 1757 Ų buried · 44 hydrogen bonds · protein-protein
- A–J · 1567 Ų buried · 19 hydrogen bonds · protein-protein
- D–G · 1550 Ų buried · 18 hydrogen bonds · protein-protein
- A–G · 648 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 3GR6 · Crystal structure of the staphylococcus aureus enoyl-acyl carrier protein reductase… · the same entry in another collection · chain J against J, TM-score 1.00
- Q6GI75 · AlphaFold monomer V2.0 prediction for enoyl-[acyl-carrier-protein] reductase [NADPH] fabi… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q6GI75
- Elsewhere: RCSB PDB 3GR6 · PDBe 3GR6 · UniProt Q6GI75
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