Research workbench
Galectin domain of porcine adenovirus type 4 nadc-1 isolate fibre complexed with TRI(N-acetyl-lactosamine)
Analyse Galectin domain of porcine adenovirus type 4 nadc-1 isolate fibre complexed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WT2
- Type
- protein
- Length
- 600 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative fiber protein
- UniProt
- Q83467
- Ligands
- NAG, GAL, NO3
- Pockets
- 5 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 1% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Putative fiber protein | protein | 300 | 1% helix, 50% strand | Q83467 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains A, B
- GAL · beta-D-galactopyranose · sugar · 6 copies · chains A, B
- NO3 · Nitrate ion · ion · 6 copies · chains A, B
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 | 376 | 0.59 | 0.76 | 40 | GAL, NAG, NO3 |
| 2 | 338 | 0.56 | 0.75 | 40 | GAL, NAG, NO3 |
| 3 | 331 | 0.53 | 0.74 | 50 | NO3 |
| 4 | 128 | 0.43 | 0.76 | 26 | NO3 |
| 5 | 50 | 0.27 | 0.74 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 134 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2WT2 · Galectin domain of porcine adenovirus type 4 NADC-1 isolate fibre complexed with… · 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 Q83467
- Elsewhere: RCSB PDB 2WT2 · PDBe 2WT2 · UniProt Q83467
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