Research workbench
Heat-labile enterotoxin lt-iib-B5(T13I) mutant
Analyse Heat-labile enterotoxin lt-iib-B5(T13I) mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FO2
- Type
- protein
- Length
- 1,960 residues
- Chains
- 20
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat-labile enterotoxin iib, B chain
- UniProt
- P43529
- Ligands
- NA
- Pockets
- 10 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D, E, F, G, H, A, B, C, I, J, K, L, M, N, O, P, Q, R, S, T | Heat-labile enterotoxin iib, B chain | protein | 98 | 27% helix, 40% strand | P43529 |
Ligands and binding sites
- NA · Sodium ion · metal · 8 copies · chains E, F, B, C, L, M, Q, R
- ACT · Acetate ion · additive · 2 copies · chains M, N, P, Q
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 877 | 0.72 | 0.77 | 65 | ACT |
| 2 | 871 | 0.72 | 0.77 | 58 | empty |
| 3 | 841 | 0.71 | 0.76 | 57 | empty |
| 4 | 834 | 0.71 | 0.76 | 57 | empty |
| 5 | 818 | 0.70 | 0.76 | 64 | NA |
Interfaces
31 interfaces between chains.
- D–E · 1236 Ų buried · 15 hydrogen bonds · protein-protein
- K–L · 1194 Ų buried · 12 hydrogen bonds · protein-protein
- P–T · 1185 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 1182 Ų buried · 15 hydrogen bonds · protein-protein
- B–C · 1182 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 disulfide (disulfide).
Compared structures
- 4FO2 · Heat-labile enterotoxin LT-IIb-B5(T13I) mutant · the same entry in another collection · chain K against K, 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 P43529
- Elsewhere: RCSB PDB 4FO2 · PDBe 4FO2 · UniProt P43529
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