Research workbench
Crystal structure analysis of the anti-testosterone Fab fragment
Analyse Crystal structure analysis of the anti-testosterone Fab fragment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1L7T
- Type
- protein
- Length
- 439 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anti-testosterone (light chain); Anti-testosterone (heavy chain)
- UniProt
- Q99M37, P01869
- Pockets
- 6 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | Anti-testosterone (light chain) | protein | 219 | 6% helix, 50% strand | Q99M37 |
| H | Anti-testosterone (heavy chain) | protein | 220 | 5% helix, 49% strand | P01869 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 507 | 0.61 | 0.75 | 49 | empty |
| 2 | 61 | 0.46 | 0.84 | 16 | empty |
| 3 | 146 | 0.46 | 0.77 | 28 | empty |
| 4 | 106 | 0.42 | 0.77 | 19 | empty |
| 5 | 90 | 0.35 | 0.75 | 20 | empty |
Interfaces
1 interface between chains.
- L–H · 2037 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 1L7T · Crystal Structure Analysis of the anti-testosterone Fab fragment · the same entry in another collection · chain L against L, TM-score 1.00
- P01869 · AlphaFold monomer V2.0 prediction for ig gamma-1 chain C region, membrane-bound form… · a predicted model of the same protein · chain H against A, TM-score 0.51
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 Q99M37
- Every structure of UniProt P01869
- Elsewhere: RCSB PDB 1L7T · PDBe 1L7T · UniProt Q99M37 · UniProt P01869
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