Research workbench
Crystal structure of S. aureus fabi in complex with NADP and 2-(2-cyanophenoxy)-5-hexylphenol
Analyse Crystal structure of S. aureus fabi in complex with NADP and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BNN
- Type
- protein
- Length
- 2,037 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enoyl-[acyl-carrier-protein] reductase [NADPH]
- EC
- 1.3.1.10
- UniProt
- Q7A6D8
- Ligands
- JUS, NAP, GLU
- Pockets
- 20 · best druggability 0.90
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, H | Enoyl-[acyl-carrier-protein] reductase [NADPH] (EC 1.3.1.10) | protein | 254 | 50% helix, 15% strand | Q7A6D8 |
| B, C, E, F, G | Enoyl-[acyl-carrier-protein] reductase [NADPH] (EC 1.3.1.10) | protein | 255 | 51% helix, 15% strand | Q7A6D8 |
Ligands and binding sites
- JUS · 2-(2-cyanophenoxy)-5-hexylphenol · ligand · 8 copies · chains A, B, C, D, E, F, G, H
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 8 copies · chains A, E, B, C, D, F, G, H
- GLU · Glutamic acid · ligand · 6 copies · chains A, E, B, C, F, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1174 | 0.90 | 0.91 | 102 | JUS, NAP |
| 2 | 1089 | 0.85 | 0.86 | 63 | empty |
| 3 | 1113 | 0.85 | 0.86 | 68 | empty |
| 4 | 545 | 0.83 | 0.88 | 50 | JUS, NAP |
| 5 | 539 | 0.83 | 0.88 | 52 | JUS, NAP |
Interfaces
15 interfaces between chains.
- G–H · 1805 Ų buried · 44 hydrogen bonds · protein-protein
- C–D · 1802 Ų buried · 41 hydrogen bonds · protein-protein
- E–F · 1788 Ų buried · 43 hydrogen bonds · protein-protein
- A–B · 1772 Ų buried · 40 hydrogen bonds · protein-protein
- B–C · 1412 Ų buried · 28 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 4BNN · Crystal structure of S. aureus FabI in complex with NADP and 2-(2… · the same entry in another collection · chain F against F, 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 Q7A6D8
- Elsewhere: RCSB PDB 4BNN · PDBe 4BNN · UniProt Q7A6D8
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