Research workbench
Crystal structure of the TV3 hybrid of human TLR4 and hagfish VLRB.61
Analyse Crystal structure of the TV3 hybrid of human TLR4 and hagfish VLRB.61 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Z62
- Type
- protein
- Length
- 276 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Toll-like receptor 4, variable lymphocyte receptor B
- UniProt
- O00206, Q4G1L2
- Ligands
- NAG, FUL, BMA
- Pockets
- 1 · best druggability 0.37
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Toll-like receptor 4, variable lymphocyte receptor B | protein | 276 | 10% helix, 19% strand | O00206, Q4G1L2 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains A
- FUL · beta-L-fucopyranose · sugar · 2 copies · chains A
- BMA · beta-D-mannopyranose · sugar
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 54 | 0.37 | 0.80 | 16 | empty |
Modifications
Observed in the structure: 3 disulfide, 3 glycan (disulfide, N-glycosylation).
Compared structures
- 2Z62 · Crystal structure of the TV3 hybrid of human TLR4 and hagfish VLRB.61 · the same entry in another collection · chain A against A, TM-score 1.00
- O00206 · AlphaFold monomer V2.0 prediction for toll-like receptor 4 (O00206) · a predicted model of the same protein · chain A against A, TM-score 0.89
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 O00206
- Every structure of UniProt Q4G1L2
- Elsewhere: RCSB PDB 2Z62 · PDBe 2Z62 · UniProt O00206 · UniProt Q4G1L2
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