Research workbench
Structure of acyl carrier protein bound to fabi, the enoyl reductase from escherichia COLI
Analyse Structure of acyl carrier protein bound to fabi, the enoyl reductase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FHS
- Type
- protein
- Length
- 568 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enoyl-[acyl-carrier-protein] reductase, NADH-dependent; Acyl carrier protein
- EC
- 1.3.1.9
- UniProt
- P0A6A8
- Pockets
- 6 · best druggability 0.62
Structure
x-ray diffraction · 3 distinct chains · 47% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enoyl-[acyl-carrier-protein] reductase, NADH-dependent (EC 1.3.1.9) | protein | 258 | 48% helix, 14% strand | — |
| B | Enoyl-[acyl-carrier-protein] reductase, NADH-dependent (EC 1.3.1.9) | protein | 253 | 47% helix, 16% strand | — |
| C | Acyl carrier protein | protein | 57 | 42% helix, 0% strand | P0A6A8 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 507 | 0.62 | 0.75 | 47 | empty |
| 2 | 379 | 0.60 | 0.76 | 43 | empty |
| 3 | 98 | 0.46 | 0.79 | 20 | empty |
| 4 | 140 | 0.40 | 0.74 | 28 | empty |
| 5 | 81 | 0.40 | 0.78 | 22 | empty |
Interfaces
2 interfaces between chains.
- A–B · 1674 Ų buried · 35 hydrogen bonds · protein-protein
- A–C · 32 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2FHS · Structure of Acyl Carrier Protein Bound to FabI, the Enoyl Reductase from Escherichia Coli · the same entry in another collection · chain A against A, TM-score 1.00
- P0A6A8 · AlphaFold monomer V2.0 prediction for acyl carrier protein (P0A6A8) · a predicted model of the same protein · chain C against A, TM-score 0.78
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 P0A6A8
- Elsewhere: RCSB PDB 2FHS · PDBe 2FHS · UniProt P0A6A8
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