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Crystal structure of teas W273S form 1
Analyse Crystal structure of teas W273S form 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HX9
- Type
- protein
- Length
- 523 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5-epi-aristolochene synthase
- EC
- 4.1.99.7
- UniProt
- Q40577
- Ligands
- FHP, MG
- Pockets
- 7 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 5-epi-aristolochene synthase (EC 4.1.99.7) | protein | 523 | 71% helix, 0% strand | Q40577 |
Ligands and binding sites
- FHP · 1-hydroxy-3,7,11-trimethyldodeca-2,6,10-triene phosphonic acid · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 555 | 0.80 | 0.86 | 49 | empty |
| 2 | 440 | 0.80 | 0.88 | 49 | FHP |
| 3 | 238 | 0.59 | 0.79 | 31 | empty |
| 4 | 267 | 0.54 | 0.76 | 28 | empty |
| 5 | 70 | 0.48 | 0.83 | 15 | empty |
Compared structures
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 1HX9 · PDBe 1HX9 · UniProt Q40577
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