MolNFT v1 · #100920 · protein
Crystal structure of fabg from acholeplasma laidlawii
4NBT · 3-oxoacyl-[acyl-carrier-protein] reductase: “Crystal structure of fabg from acholeplasma laidlawii”. X-ray diffraction, 1 ligand (NAD), 9 pockets (best druggability 0.83). MolNFT v1 #100920 on GenesisL1: 3D structure, binding sites…
- PDB
- 4NBT
- Type
- protein
- Length
- 956 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-oxoacyl-[acyl-carrier-protein] reductase
- EC
- 1.1.1.100
- UniProt
- A9NFJ2
- Ligands
- NAD
- Pockets
- 9 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) | protein | 239 | 46% helix, 18% strand | A9NFJ2 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1142 | 0.83 | 0.84 | 74 | empty |
| 2 | 621 | 0.73 | 0.80 | 77 | NAD |
| 3 | 659 | 0.73 | 0.80 | 78 | NAD |
| 4 | 466 | 0.72 | 0.81 | 45 | NAD |
| 5 | 485 | 0.70 | 0.80 | 40 | NAD |
Interfaces
6 interfaces between chains.
- B–C · 1703 Ų buried · 27 hydrogen bonds · protein-protein
- A–D · 1681 Ų buried · 25 hydrogen bonds · protein-protein
- A–B · 1432 Ų buried · 18 hydrogen bonds · protein-protein
- C–D · 1417 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 171 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 4NBT · Crystal structure of FabG from Acholeplasma laidlawii · 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 A9NFJ2
- Elsewhere: RCSB PDB 4NBT · PDBe 4NBT · UniProt A9NFJ2
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