Research workbench
Crystal structure of the complex of goat signalling protein with tetrasaccharide at 2.09 a resolution
Analyse Crystal structure of the complex of goat signalling protein with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2DT1
- Type
- protein
- Length
- 361 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chitinase-3-like protein 1
- UniProt
- Q8SPQ0
- Ligands
- NAG, NDG, BMA
- Pockets
- 3 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chitinase-3-like protein 1 | protein | 361 | 37% helix, 24% strand | Q8SPQ0 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A
- NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar
- BMA · beta-D-mannopyranose · sugar
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 | 258 | 0.58 | 0.78 | 40 | NAG |
| 2 | 207 | 0.55 | 0.79 | 27 | empty |
| 3 | 91 | 0.35 | 0.74 | 17 | empty |
Modifications
Observed in the structure: 2 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 2DT1 · Crystal Structure Of The Complex Of Goat Signalling Protein With Tetrasaccharide At 2.09… · the same entry in another collection · chain A against A, TM-score 1.00
- Q8SPQ0 · AlphaFold monomer V2.0 prediction for chitinase-3-like protein 1 (Q8SPQ0) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q8SPQ0
- Elsewhere: RCSB PDB 2DT1 · PDBe 2DT1 · UniProt Q8SPQ0
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