Research workbench
Crystal structure of yeast 4-amino-4-deoxychorismate lyase
Analyse Crystal structure of yeast 4-amino-4-deoxychorismate lyase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4K6N
- Type
- protein
- Length
- 352 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aminodeoxychorismate lyase
- EC
- 4.1.3.38
- UniProt
- Q03266
- Ligands
- PLP
- Pockets
- 4 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aminodeoxychorismate lyase (EC 4.1.3.38) | protein | 352 | 37% helix, 25% strand | Q03266 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 344 | 0.62 | 0.78 | 49 | PLP |
| 2 | 96 | 0.47 | 0.81 | 25 | empty |
| 3 | 78 | 0.46 | 0.82 | 21 | empty |
| 4 | 98 | 0.39 | 0.77 | 21 | empty |
Modifications
Observed in the structure: 1 cofactor (pyridoxal phosphate Schiff base).
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 Q03266
- Elsewhere: RCSB PDB 4K6N · PDBe 4K6N · UniProt Q03266
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.