Research workbench
Crystal structure of enoyl-acyl carrier protein reductase (fabi) from neisseria meningitidis in complex with NAD+ and triclosan
Analyse Crystal structure of enoyl-acyl carrier protein reductase (fabi) from neisseria… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4M89
- Type
- protein
- Length
- 514 residues
- Chains
- 2
- 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
- A1KVU8
- Ligands
- NAD, TCL
- Pockets
- 5 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 257 | 50% helix, 14% strand | A1KVU8 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B
- TCL · Triclosan · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 484 | 0.80 | 0.87 | 46 | NAD, TCL |
| 2 | 495 | 0.79 | 0.86 | 44 | NAD, TCL |
| 3 | 206 | 0.47 | 0.74 | 22 | empty |
| 4 | 64 | 0.38 | 0.79 | 21 | empty |
| 5 | 60 | 0.32 | 0.75 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1333 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 4M89 · Crystal Structure of Enoyl-Acyl Carrier Protein Reductase (FabI) from Neisseria… · 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 A1KVU8
- Elsewhere: RCSB PDB 4M89 · PDBe 4M89 · UniProt A1KVU8
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