Research workbench
Crystal structure of the anst-D7L1-U46619 complex
Analyse Crystal structure of the anst-D7L1-U46619 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3NHT
- Type
- protein
- Length
- 295 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- D7 protein
- UniProt
- Q95NY5
- Ligands
- U46, SO4
- Pockets
- 3 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 59% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | D7 protein | protein | 295 | 59% helix, 3% strand | Q95NY5 |
Ligands and binding sites
- U46 · (5E)-7-{6-[(1E)-3-hydroxyoct-1-enyl]-2-oxabicyclo[2.2.1]hept-5-yl}hept-5-enoic acid · ligand · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 288 | 0.67 | 0.82 | 42 | U46 |
| 2 | 358 | 0.54 | 0.74 | 34 | empty |
| 3 | 51 | 0.35 | 0.80 | 13 | empty |
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 3NHT · Crystal structure of the AnSt-D7L1-U46619 complex · 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 Q95NY5
- Elsewhere: RCSB PDB 3NHT · PDBe 3NHT · UniProt Q95NY5
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