Research workbench
Choristoneura fumiferana (spruce budworm) antifreeze protein isoform 337
Analyse Choristoneura fumiferana (spruce budworm) antifreeze protein isoform 337 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1L0S
- Type
- protein
- Length
- 352 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thermal hysteresis protein
- UniProt
- Q9GTP0
- Ligands
- CD
- Pockets
- 3 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 66% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Thermal hysteresis protein | protein | 88 | 0% helix, 66% strand | Q9GTP0 |
Ligands and binding sites
- CD · Cadmium ion · metal · 2 copies · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 145 | 0.46 | 0.77 | 26 | empty |
| 2 | 105 | 0.37 | 0.75 | 19 | empty |
| 3 | 78 | 0.37 | 0.78 | 19 | empty |
Interfaces
4 interfaces between chains.
- A–B · 599 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 585 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 364 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 14 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 disulfide, 4 modified (disulfide, nonstandard).
Compared structures
- 1L0S · Choristoneura fumiferana (spruce budworm) antifreeze protein isoform 337 · 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 Q9GTP0
- Elsewhere: RCSB PDB 1L0S · PDBe 1L0S · UniProt Q9GTP0
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.