MolNFT v1 · #180131 · protein
Structure of isethionate sulfite-lyase from bilophila wadsworthia with substrate isethionate bound
7KQ3: “Structure of isethionate sulfite-lyase from bilophila wadsworthia with substrate isethionate bound”. X-ray diffraction, 1 ligand (8X3), 20 pockets (best druggability 0.81). MolNFT v1 #180131 on GenesisL1: 3D structure, binding sites…
- PDB
- 7KQ3
- Type
- protein
- Length
- 3,300 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Isethionate sulfite-lyase
- EC
- 4.4.1.-
- UniProt
- E5Y378
- Ligands
- 8X3
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Isethionate sulfite-lyase (EC 4.4.1.-) | protein | 825 | 52% helix, 10% strand | E5Y378 |
Ligands and binding sites
- 8X3 · 2-hydroxyethylsulfonic acid · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 877 | 0.81 | 0.83 | 105 | empty |
| 2 | 1160 | 0.80 | 0.81 | 92 | empty |
| 3 | 292 | 0.78 | 0.89 | 50 | empty |
| 4 | 295 | 0.75 | 0.87 | 58 | empty |
| 5 | 157 | 0.66 | 0.87 | 27 | empty |
Interfaces
4 interfaces between chains.
- A–B · 1128 Ų buried · 12 hydrogen bonds · protein-protein
- C–D · 1123 Ų buried · 15 hydrogen bonds · protein-protein
- B–C · 1083 Ų buried · 15 hydrogen bonds · protein-protein
- A–D · 1066 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 7KQ3 · Structure of isethionate sulfite-lyase from Bilophila wadsworthia with substrate… · the same entry in another collection · chain A against A, TM-score 1.00
- E5Y378 · AlphaFold monomer V2.0 prediction for isethionate sulfite-lyase (E5Y378) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 E5Y378
- Elsewhere: RCSB PDB 7KQ3 · PDBe 7KQ3 · UniProt E5Y378
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