Research workbench
Saccharomyces cerevisiae GAS2P (E176Q mutant) in complex with laminaritetraose and laminaripentaose
Analyse Saccharomyces cerevisiae GAS2P (E176Q mutant) in complex with laminaritetraose… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FIH
- Type
- protein
- Length
- 438 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 1,3-beta-glucanosyltransferase
- EC
- 2.4.1.-
- UniProt
- N1P1N2
- Ligands
- BGC, GLC
- Pockets
- 4 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 1,3-beta-glucanosyltransferase (EC 2.4.1.-) | protein | 438 | 35% helix, 17% strand | N1P1N2 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 7 copies · chains A
- GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 216 | 0.52 | 0.76 | 29 | empty |
| 2 | 160 | 0.48 | 0.77 | 25 | BGC |
| 3 | 122 | 0.47 | 0.78 | 23 | empty |
| 4 | 83 | 0.30 | 0.72 | 17 | empty |
Modifications
Observed in the structure: 7 disulfide, 1 glycan (disulfide, glycosylation).
Compared structures
- 5FIH · Saccharomyces cerevisiae GAS2P (E176Q mutant) in complex with laminaritetraose and… · 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 N1P1N2
- Elsewhere: RCSB PDB 5FIH · PDBe 5FIH · UniProt N1P1N2
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