MolNFT v1 · #19149 · protein
Escherichia COLI heat labile enterotoxin type iib B-pentamer
1QB5 · Protein (heat labile enterotoxin type iib B- pentamer): “Escherichia COLI heat labile enterotoxin type iib B-pentamer”. X-ray diffraction, 1 pocket (best druggability 0.72). MolNFT v1 #19149 on GenesisL1: 3D structure, binding sites…
- PDB
- 1QB5
- Type
- protein
- Length
- 495 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (heat labile enterotoxin type iib B- pentamer)
- UniProt
- P43529
- Pockets
- 1 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D, E, F, G, H | Protein (heat labile enterotoxin type iib B- pentamer) | protein | 99 | 26% helix, 37% strand | P43529 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 887 | 0.72 | 0.77 | 62 | empty |
Interfaces
5 interfaces between chains.
- D–E · 1271 Ų buried · 16 hydrogen bonds · protein-protein
- E–F · 1260 Ų buried · 19 hydrogen bonds · protein-protein
- G–H · 1213 Ų buried · 19 hydrogen bonds · protein-protein
- F–G · 1206 Ų buried · 19 hydrogen bonds · protein-protein
- D–H · 1193 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 1QB5 · Escherichia COLI heat labile enterotoxin type iib B-pentamer · the same entry in another collection · chain H against H, TM-score 1.00
- P43529 · AlphaFold monomer V2.0 prediction for heat-labile enterotoxin iib, B chain (P43529) · a predicted model of the same protein · chain H against A, TM-score 0.99
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 P43529
- Elsewhere: RCSB PDB 1QB5 · PDBe 1QB5 · UniProt P43529
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