Research workbench
A372M mutant of enoyl-acp reductase from plasmodium falciparum (pfenr) in complex with triclosan variant T1
Analyse A372M mutant of enoyl-acp reductase from plasmodium falciparum (pfenr) in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3AM4
- Type
- protein
- Length
- 574 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enoyl-acp reductase
- EC
- 1.3.1.9
- UniProt
- Q9BJJ9
- Ligands
- NAD, FT1
- Pockets
- 7 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Enoyl-acp reductase (EC 1.3.1.9) | protein | 287 | 47% helix, 18% strand | Q9BJJ9 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B
- FT1 · 4-(2,4-dichlorophenoxy)-3-hydroxybenzaldehyde · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 562 | 0.82 | 0.87 | 45 | NAD, FT1 |
| 2 | 534 | 0.80 | 0.87 | 48 | NAD, FT1 |
| 3 | 147 | 0.55 | 0.81 | 26 | empty |
| 4 | 167 | 0.54 | 0.80 | 23 | empty |
| 5 | 271 | 0.54 | 0.76 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 1696 Ų buried · 37 hydrogen bonds · protein-protein
Compared structures
- 3AM4 · A372M mutant of Enoyl-ACP Reductase from Plasmodium falciparum (PfENR) in 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 Q9BJJ9
- Elsewhere: RCSB PDB 3AM4 · PDBe 3AM4 · UniProt Q9BJJ9
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.