Research workbench
Crystal structure of na-asp-1
Analyse Crystal structure of na-asp-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3NT8
- Type
- protein
- Length
- 800 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ancylostoma secreted protein 1
- UniProt
- O76744
- Pockets
- 7 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ancylostoma secreted protein 1 | protein | 401 | 29% helix, 20% strand | O76744 |
| B | Ancylostoma secreted protein 1 | protein | 399 | 30% helix, 19% strand | O76744 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1056 | 0.71 | 0.75 | 94 | empty |
| 2 | 703 | 0.67 | 0.76 | 65 | empty |
| 3 | 461 | 0.60 | 0.75 | 51 | empty |
| 4 | 130 | 0.40 | 0.74 | 17 | empty |
| 5 | 85 | 0.38 | 0.78 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 490 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 disulfide (disulfide).
Compared structures
- 3NT8 · Crystal Structure of Na-ASP-1 · the same entry in another collection · chain A against A, 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
- Every structure of UniProt O76744
- Elsewhere: RCSB PDB 3NT8 · PDBe 3NT8 · UniProt O76744
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