MolNFT v1 · #173061 · protein
Enzyme of biosynthetic pathway
7AN9 · Chorismate dehydratase: “Enzyme of biosynthetic pathway”. X-ray diffraction, 1 ligand (RDH), 5 pockets (best druggability 0.75). MolNFT v1 #173061 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7AN9
- Type
- protein
- Length
- 558 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chorismate dehydratase
- EC
- 4.2.1.151
- UniProt
- Q9L0T8
- Ligands
- RDH
- Pockets
- 5 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chorismate dehydratase (EC 4.2.1.151) | protein | 280 | 51% helix, 22% strand | Q9L0T8 |
| B | Chorismate dehydratase (EC 4.2.1.151) | protein | 278 | 52% helix, 22% strand | Q9L0T8 |
Ligands and binding sites
- RDH · 3-[(1-Carboxyvinyl)oxy]benzoic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 66 | 0.75 | 0.99 | 20 | RDH |
| 2 | 63 | 0.74 | 0.99 | 19 | RDH |
| 3 | 374 | 0.60 | 0.76 | 40 | empty |
| 4 | 91 | 0.38 | 0.76 | 18 | empty |
| 5 | 81 | 0.37 | 0.76 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 953 Ų buried · 20 hydrogen bonds · protein-protein
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 Q9L0T8
- Elsewhere: RCSB PDB 7AN9 · PDBe 7AN9 · UniProt Q9L0T8
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