Research workbench
Human ASIC1A-NB.C1 complex
Analyse Human ASIC1A-NB.C1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RNN
- Type
- protein
- Length
- 540 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nanobodies NB.C1; Acid-sensing ion channel 1
- UniProt
- P78348
- Ligands
- NAG
- Pockets
- 5 · best druggability 0.65
Structure
electron microscopy · 2 distinct chains · 27% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | Nanobodies NB.C1 | protein | 116 | 5% helix, 42% strand | — |
| D | Acid-sensing ion channel 1 | protein | 424 | 33% helix, 24% strand | P78348 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 380 | 0.65 | 0.79 | 39 | empty |
| 2 | 196 | 0.57 | 0.80 | 36 | empty |
| 3 | 113 | 0.56 | 0.84 | 24 | empty |
| 4 | 172 | 0.49 | 0.77 | 32 | empty |
| 5 | 60 | 0.31 | 0.75 | 14 | empty |
Interfaces
1 interface between chains.
- C–D · 640 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 disulfide, 2 glycan (disulfide, N-glycosylation).
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 P78348
- Elsewhere: RCSB PDB 7RNN · PDBe 7RNN · UniProt P78348
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