Research workbench
Fab antigen complex
Analyse Fab antigen complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6WIR
- Type
- protein
- Length
- 528 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fab heavy chain; Fab light chain; Interleukin-17A
- UniProt
- Q16552
- Pockets
- 4 · best druggability 0.56
Structure
x-ray diffraction · 3 distinct chains · 6% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fab heavy chain | protein | 227 | 7% helix, 52% strand | — |
| B | Fab light chain | protein | 212 | 7% helix, 55% strand | — |
| C | Interleukin-17A | protein | 89 | 4% helix, 44% strand | Q16552 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 359 | 0.56 | 0.75 | 45 | empty |
| 2 | 96 | 0.45 | 0.79 | 21 | empty |
| 3 | 88 | 0.36 | 0.75 | 19 | empty |
| 4 | 78 | 0.31 | 0.74 | 18 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1752 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 469 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 235 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
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 Q16552
- Elsewhere: RCSB PDB 6WIR · PDBe 6WIR · UniProt Q16552
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