Research workbench
HASIC1A co-crystallized with mamb-1
Analyse HASIC1A co-crystallized with mamb-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6L6I
- Type
- protein
- Length
- 1,281 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acid-sensing ion channel 1
- UniProt
- P78348
- Ligands
- NAG
- Pockets
- 19 · best druggability 0.86
Structure
x-ray diffraction · 3 distinct chains · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acid-sensing ion channel 1 | protein | 428 | 37% helix, 24% strand | P78348 |
| B | Acid-sensing ion channel 1 | protein | 443 | 38% helix, 23% strand | P78348 |
| C | Acid-sensing ion channel 1 | protein | 410 | 35% helix, 25% strand | P78348 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 885 | 0.86 | 0.88 | 109 | empty |
| 2 | 799 | 0.83 | 0.85 | 70 | empty |
| 3 | 409 | 0.82 | 0.90 | 59 | empty |
| 4 | 514 | 0.79 | 0.86 | 62 | empty |
| 5 | 145 | 0.78 | 0.95 | 42 | empty |
Interfaces
3 interfaces between chains.
- A–B · 2786 Ų buried · 21 hydrogen bonds · protein-protein
- B–C · 2486 Ų buried · 26 hydrogen bonds · protein-protein
- A–C · 2373 Ų buried · 22 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 21 disulfide, 3 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 6L6I · PDBe 6L6I · UniProt P78348
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