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2 beta-glucans (6-O-glucosyl-laminaritriose) in both donor and acceptor sites of GH16 laminarinase 16A from phanerochaete chrysosporium.
Analyse 2 beta-glucans (6-O-glucosyl-laminaritriose) in both donor and acceptor sites… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2W52
- Type
- protein
- Length
- 298 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative laminarinase
- EC
- 3.2.1.6
- UniProt
- Q874E3
- Ligands
- BGC, MAN, NAG, BMA
- Pockets
- 1 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative laminarinase (EC 3.2.1.6) | protein | 298 | 20% helix, 38% strand | Q874E3 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 7 copies · chains A
- MAN · alpha-D-mannopyranose · sugar · 4 copies · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
- BMA · beta-D-mannopyranose · sugar
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 282 | 0.60 | 0.79 | 39 | BGC |
Modifications
Observed in the structure: 4 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 2W52 · 2 beta-glucans (6-O-glucosyl-laminaritriose) in both donor and acceptor sites of GH16… · 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 Q874E3
- Elsewhere: RCSB PDB 2W52 · PDBe 2W52 · UniProt Q874E3
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