Research workbench
Crystal structure of human heat-labile enterotoxin in complex with a blood group a antigen analog
Analyse Crystal structure of human heat-labile enterotoxin in complex with a blood… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2O2L
- Type
- protein
- Length
- 1,012 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat-labile enterotoxin B chain
- UniProt
- P13811
- Ligands
- FUC, BGC, GAL, A2G
- Pockets
- 9 · best druggability 0.77
Structure
x-ray diffraction · 6 distinct chains · 24% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D | Heat-labile enterotoxin B chain | protein | 98 | 24% helix, 38% strand | P13811 |
| E, F, I, J, K | Heat-labile enterotoxin B chain | protein | 103 | 24% helix, 37% strand | P13811 |
| G | Heat-labile enterotoxin B chain | protein | 100 | 26% helix, 42% strand | P13811 |
| H | Heat-labile enterotoxin B chain | protein | 99 | 23% helix, 38% strand | P13811 |
| L | Heat-labile enterotoxin B chain | protein | 99 | 24% helix, 38% strand | P13811 |
| M | Heat-labile enterotoxin B chain | protein | 101 | 24% helix, 39% strand | P13811 |
Ligands and binding sites
- FUC · alpha-L-fucopyranose · sugar · 20 copies · chains D, H, E, F, G, I, M, J, K, L
- BGC · beta-D-glucopyranose · sugar · 10 copies · chains D, E, F, G, H, I, J, K, L, M
- GAL · beta-D-galactopyranose · sugar · 10 copies · chains D, K, E, F, G, H, I, J, L, M
- A2G · 2-acetamido-2-deoxy-alpha-D-galactopyranose · sugar · 10 copies · chains D, H, K, E, F, G, I, M, J, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 950 | 0.77 | 0.79 | 42 | empty |
| 2 | 1130 | 0.75 | 0.78 | 46 | empty |
| 3 | 662 | 0.75 | 0.81 | 76 | GAL, FUC, A2G |
| 4 | 53 | 0.40 | 0.82 | 18 | empty |
| 5 | 55 | 0.39 | 0.81 | 18 | empty |
Interfaces
13 interfaces between chains.
- F–G · 1406 Ų buried · 29 hydrogen bonds · protein-protein
- I–M · 1399 Ų buried · 29 hydrogen bonds · protein-protein
- K–L · 1386 Ų buried · 29 hydrogen bonds · protein-protein
- D–E · 1386 Ų buried · 27 hydrogen bonds · protein-protein
- L–M · 1364 Ų buried · 29 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2O2L · Crystal structure of human heat-labile enterotoxin in complex with a blood group A… · the same entry in another collection · chain D against D, 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 P13811
- Elsewhere: RCSB PDB 2O2L · PDBe 2O2L · UniProt P13811
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.