MolNFT v1 · #35212 · protein
X-ray crystal structure of aristolochene synthase from aspergillus terreus and the evolution of templates for the cyclization of farnesyl diphosphate
2E4O: “X-ray crystal structure of aristolochene synthase from aspergillus terreus and the evolution of templates for…”. X-ray diffraction, 1 ligand (CL), 20 pockets (best druggability 0.82). MolNFT v1 #35212 on GenesisL1: 3D structure…
- PDB
- 2E4O
- Type
- protein
- Length
- 1,180 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aristolochene synthase
- EC
- 4.2.3.9
- UniProt
- Q9UR08
- Ligands
- CL
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 4 distinct chains · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aristolochene synthase (EC 4.2.3.9) | protein | 295 | 74% helix, 0% strand | Q9UR08 |
| B | Aristolochene synthase (EC 4.2.3.9) | protein | 295 | 72% helix, 0% strand | Q9UR08 |
| C | Aristolochene synthase (EC 4.2.3.9) | protein | 296 | 71% helix, 0% strand | Q9UR08 |
| D | Aristolochene synthase (EC 4.2.3.9) | protein | 294 | 71% helix, 0% strand | Q9UR08 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains B, C
- BME · Beta-mercaptoethanol · additive · 5 copies · chains A, C, D
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 819 | 0.82 | 0.84 | 91 | CL |
| 2 | 228 | 0.81 | 0.94 | 32 | empty |
| 3 | 461 | 0.75 | 0.84 | 34 | MES |
| 4 | 348 | 0.74 | 0.85 | 31 | empty |
| 5 | 431 | 0.74 | 0.84 | 33 | CL |
Interfaces
6 interfaces between chains.
- B–C · 875 Ų buried · 15 hydrogen bonds · protein-protein
- A–D · 875 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 652 Ų buried · 9 hydrogen bonds · protein-protein
- B–D · 577 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 426 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 4 covalent (additive adduct).
Compared structures
- 2E4O · X-ray Crystal Structure of Aristolochene Synthase from Aspergillus terreus and the… · the same entry in another collection · chain D against D, TM-score 1.00
- Q9UR08 · AlphaFold monomer V2.0 prediction for aristolochene synthase (Q9UR08) · a predicted model of the same protein · chain D against A, TM-score 0.94
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 Q9UR08
- Elsewhere: RCSB PDB 2E4O · PDBe 2E4O · UniProt Q9UR08
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