MolNFT v1 · #70959 · protein
Crystal structure of 5-epi-aristolochene synthase M4 mutant complexed with (2-CIS,6-trans)-2-fluorofarnesyl diphosphate
3M00: “Crystal structure of 5-epi-aristolochene synthase M4 mutant complexed with (2-CIS,6-trans)-2-fluorofarnesyl…”. X-ray diffraction, 2 ligands (2CF, MG), 6 pockets (best druggability 0.80). MolNFT v1 #70959 on GenesisL1: 3D structure…
- PDB
- 3M00
- Type
- protein
- Length
- 530 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 0.80
Structure
x-ray diffraction · 1 distinct chain · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aristolochene synthase (EC 4.2.3.9) | protein | 530 | 72% 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 | 768 | 0.80 | 0.84 | 64 | 2CF, MG |
| 2 | 512 | 0.79 | 0.86 | 43 | empty |
| 3 | 227 | 0.57 | 0.79 | 26 | empty |
| 4 | 261 | 0.53 | 0.76 | 29 | empty |
| 5 | 86 | 0.43 | 0.79 | 15 | empty |
Compared structures
- 3M00 · Crystal Structure of 5-epi-aristolochene synthase M4 mutant 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 3M00 · PDBe 3M00 · UniProt Q40577
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.