Research workbench
Crystal structure of anti-tau antibody PT3 FAB+PT212/PT217-tau peptide
Analyse Crystal structure of anti-tau antibody PT3 FAB+PT212/PT217-tau peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XLI
- Type
- protein
- Length
- 1,312 residues
- Chains
- 9
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- PT3 Fab heavy chain; PT3 Fab light chain; Tau phosphopeptide (ac-SR(PT)PSLP(PT)PPTRE-oh)
- UniProt
- P10636
- Pockets
- 20 · best druggability 0.61
Structure
x-ray diffraction · 6 distinct chains · 7% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | PT3 Fab heavy chain | protein | 207 | 9% helix, 53% strand | — |
| B | PT3 Fab light chain | protein | 212 | 5% helix, 51% strand | — |
| C | PT3 Fab heavy chain | protein | 213 | 9% helix, 54% strand | — |
| D, L | PT3 Fab light chain | protein | 213 | 6% helix, 51% strand | — |
| H | PT3 Fab heavy chain | protein | 215 | 9% helix, 54% strand | — |
| E, F, P | Tau phosphopeptide (ac-SR(PT)PSLP(PT)PPTRE-oh) | protein | 13 | 0% helix, 8% strand | P10636 |
Ligands and binding sites
- GOL · Glycerol · additive · 3 copies · chains A, B, C, D, H, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 437 | 0.61 | 0.76 | 50 | empty |
| 2 | 56 | 0.55 | 0.89 | 21 | GOL |
| 3 | 345 | 0.54 | 0.74 | 45 | empty |
| 4 | 62 | 0.52 | 0.87 | 22 | GOL |
| 5 | 52 | 0.52 | 0.88 | 21 | GOL |
Interfaces
15 interfaces between chains.
- A–B · 1878 Ų buried · 21 hydrogen bonds · protein-protein
- C–D · 1861 Ų buried · 18 hydrogen bonds · protein-protein
- H–L · 1835 Ų buried · 18 hydrogen bonds · protein-protein
- C–F · 621 Ų buried · 12 hydrogen bonds · protein-protein
- H–P · 620 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 disulfide, 6 modified (disulfide, phosphorylation).
Compared structures
- 6XLI · CRYSTAL STRUCTURE OF ANTI-TAU ANTIBODY PT3 Fab+pT212/pT217-TAU PEPTIDE · the same entry in another collection · chain C against C, 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 P10636
- Elsewhere: RCSB PDB 6XLI · PDBe 6XLI · UniProt P10636
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.