MolNFT v1 · #70961 · protein
The crystal structure of 5-epi-aristolochene synthase complexed with (2-CIS,6-trans)-2-fluorofarnesyl diphosphate
3M02: “The crystal structure of 5-epi-aristolochene synthase complexed with (2-CIS,6-trans)-2-fluorofarnesyl…”. X-ray diffraction, 2 ligands (2CF, MG), 6 pockets (best druggability 0.81). MolNFT v1 #70961 on GenesisL1: 3D structure…
- PDB
- 3M02
- Type
- protein
- Length
- 535 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aristolochene synthase
- EC
- 4.2.3.9
- UniProt
- Q40577
- Ligands
- 2CF, MG
- Pockets
- 6 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aristolochene synthase (EC 4.2.3.9) | protein | 535 | 71% helix, 0% strand | Q40577 |
Ligands and binding sites
- 2CF · (2E,6E)-2-fluoro-3,7,11-trimethyldodeca-2,6,10-trien-1-yl trihydrogen diphosphate · ligand · chains A
- MG · Magnesium ion · metal · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 875 | 0.81 | 0.83 | 82 | MG, 2CF |
| 2 | 450 | 0.79 | 0.87 | 40 | empty |
| 3 | 259 | 0.55 | 0.77 | 30 | empty |
| 4 | 182 | 0.54 | 0.79 | 20 | empty |
| 5 | 112 | 0.40 | 0.75 | 17 | empty |
Compared structures
- 3M02 · The Crystal Structure of 5-epi-aristolochene synthase complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
- Q40577 · AlphaFold monomer V2.0 prediction for 5-epi-aristolochene synthase (Q40577) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q40577
- Elsewhere: RCSB PDB 3M02 · PDBe 3M02 · UniProt Q40577
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