Research workbench
Structural evidence for induced fit as a mechanism for antibody-antigen recognition
Analyse Structural evidence for induced fit as a mechanism for antibody-antigen… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HIN
- Type
- protein
- Length
- 445 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- IGG2A-kappa 17/9 Fab (light chain); IGG2A-kappa 17/9 Fab (heavy chain); Influenza…
- Pockets
- 3 · best druggability 0.54
Structure
x-ray diffraction · 3 distinct chains · 6% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | IGG2A-kappa 17/9 Fab (light chain) | protein | 217 | 6% helix, 49% strand | — |
| H | IGG2A-kappa 17/9 Fab (heavy chain) | protein | 220 | 6% helix, 45% strand | — |
| P | Influenza hemagglutinin HA1 (strain X47) (residues 100-107) | protein | 8 | 0% helix, 0% strand | — |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 340 | 0.54 | 0.74 | 50 | empty |
| 2 | 79 | 0.35 | 0.76 | 20 | empty |
| 3 | 59 | 0.32 | 0.76 | 16 | empty |
Interfaces
3 interfaces between chains.
- L–H · 1760 Ų buried · 15 hydrogen bonds · protein-protein
- H–P · 482 Ų buried · 11 hydrogen bonds · protein-protein
- L–P · 187 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1HIN · Structural evidence for induced fit as a mechanism for antibody-antigen recognition · the same entry in another collection · chain L against L, 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
- Elsewhere: RCSB PDB 1HIN · PDBe 1HIN
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