MolNFT v1 · #73956 · protein
Crystal structure of enoyl-acp reductases I (fabi) from B. subtilis (complex with NAD and tcl)
3OIF · Enoyl-[acyl-carrier-protein] reductase [NADH]: “Crystal structure of enoyl-acp reductases I (fabi) from B. subtilis (complex with NAD and tcl)”. X-ray diffraction, 2 ligands (NAD, TCL), 11 pockets (best druggability 0.80). MolNFT v1…
- PDB
- 3OIF
- Type
- protein
- Length
- 984 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
- P54616
- Ligands
- NAD, TCL
- Pockets
- 11 · best druggability 0.80
Structure
x-ray diffraction · 4 distinct chains · 48% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 258 | 46% helix, 15% strand | P54616 |
| B | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 228 | 50% helix, 17% strand | P54616 |
| C | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 241 | 51% helix, 16% strand | P54616 |
| D | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 257 | 46% helix, 15% strand | P54616 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, D
- TCL · Triclosan · ligand · 2 copies · chains A, 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, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 622 | 0.80 | 0.85 | 51 | NAD, TCL |
| 2 | 1193 | 0.78 | 0.80 | 85 | empty |
| 3 | 723 | 0.78 | 0.82 | 70 | NAD, TCL |
| 4 | 199 | 0.55 | 0.79 | 30 | empty |
| 5 | 265 | 0.51 | 0.74 | 34 | empty |
Interfaces
6 interfaces between chains.
- A–D · 1704 Ų buried · 37 hydrogen bonds · protein-protein
- B–C · 1592 Ų buried · 33 hydrogen bonds · protein-protein
- C–D · 1581 Ų buried · 23 hydrogen bonds · protein-protein
- A–B · 1571 Ų buried · 26 hydrogen bonds · protein-protein
- A–C · 387 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 3OIF · Crystal Structure of Enoyl-ACP Reductases I (FabI) from B. subtilis (complex with NAD and… · the same entry in another collection · chain D against D, TM-score 1.00
- P54616 · AlphaFold monomer V2.0 prediction for enoyl-[acyl-carrier-protein] reductase [NADH] fabi… · a predicted model of the same protein · chain C 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 P54616
- Elsewhere: RCSB PDB 3OIF · PDBe 3OIF · UniProt P54616
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