Research workbench
Crystal structure of fabi from candidatus liberibacter asiaticus
Analyse Crystal structure of fabi from candidatus liberibacter asiaticus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NK4
- Type
- protein
- Length
- 1,547 residues
- Chains
- 6
- 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
- M4Q2P0
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 258 | 50% helix, 14% strand | M4Q2P0 |
| F | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 257 | 48% helix, 15% strand | M4Q2P0 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · 10 copies · chains A, B, C, E, D, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 900 | 0.86 | 0.88 | 94 | PEG |
| 2 | 660 | 0.81 | 0.85 | 56 | PEG |
| 3 | 753 | 0.80 | 0.84 | 81 | PEG |
| 4 | 499 | 0.79 | 0.86 | 45 | empty |
| 5 | 454 | 0.78 | 0.86 | 39 | PEG |
Interfaces
9 interfaces between chains.
- E–F · 1664 Ų buried · 29 hydrogen bonds · protein-protein
- A–B · 1625 Ų buried · 28 hydrogen bonds · protein-protein
- D–E · 1619 Ų buried · 26 hydrogen bonds · protein-protein
- C–D · 1594 Ų buried · 29 hydrogen bonds · protein-protein
- C–F · 1522 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 4NK4 · Crystal structure of FabI from Candidatus Liberibacter asiaticus · 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 M4Q2P0
- Elsewhere: RCSB PDB 4NK4 · PDBe 4NK4 · UniProt M4Q2P0
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