Research workbench
Crystal structure of the mrh domain of glucosidase II beta bound to mannose
Analyse Crystal structure of the mrh domain of glucosidase II beta bound to mannose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4XQM
- Type
- protein
- Length
- 94 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucosidase 2 subunit beta
- EC
- 3.2.1.84
- UniProt
- Q9USH8
- Ligands
- MAN
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 61% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucosidase 2 subunit beta (EC 3.2.1.84) | protein | 94 | 3% helix, 61% strand | Q9USH8 |
Ligands and binding sites
- MAN · alpha-D-mannopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4XQM · Crystal structure of the MRH domain of Glucosidase II beta bound to mannose · the same entry in another collection · chain A against A, TM-score 1.00
- Q9USH8 · AlphaFold monomer V2.0 prediction for glucosidase 2 subunit beta (Q9USH8) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q9USH8
- Elsewhere: RCSB PDB 4XQM · PDBe 4XQM · UniProt Q9USH8
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