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GLC(BETA-1-3)GLC disaccharide in -1 and -2 sites of laminarinase 16A from phanerochaete chrysosporium
Analyse GLC(BETA-1-3)GLC disaccharide in -1 and -2 sites of laminarinase 16A from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2W39
- 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
- LGC, BGC, NAG
- Pockets
- 1 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 21% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative laminarinase (EC 3.2.1.6) | protein | 298 | 21% helix, 39% strand | Q874E3 |
Ligands and binding sites
- LGC · D-glucono-1,5-lactone · ligand · chains A
- BGC · beta-D-glucopyranose · sugar · 2 copies · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
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 | 242 | 0.57 | 0.79 | 38 | BGC, LGC |
Modifications
Observed in the structure: 4 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 2W39 · Glc(beta-1-3)Glc disaccharide in -1 and -2 sites of Laminarinase 16A from Phanerochaete… · 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 2W39 · PDBe 2W39 · UniProt Q874E3
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