MolNFT v1 · #123642 · protein
Crystal structure of er glucosidase II heterodimeric complex consisting of catalytic subunit and the binding domain of regulatory subunit
5JQP · Alpha glucosidase-like protein: “Crystal structure of er glucosidase II heterodimeric complex consisting of catalytic subunit and the binding…”. X-ray diffraction, 1 ligand (CA), 14 pockets (best druggability 0.67). MolNFT v1…
- PDB
- 5JQP
- Type
- protein
- Length
- 1,049 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha glucosidase-like protein; Glucosidase 2 subunit beta-like protein
- UniProt
- G0SG42, G0S9M2
- Ligands
- CA
- Pockets
- 14 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 21% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha glucosidase-like protein | protein | 918 | 22% helix, 30% strand | G0SG42 |
| B | Glucosidase 2 subunit beta-like protein | protein | 131 | 14% helix, 11% strand | G0S9M2 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains B, A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 190 | 0.67 | 0.86 | 45 | empty |
| 2 | 208 | 0.65 | 0.84 | 33 | empty |
| 3 | 306 | 0.62 | 0.79 | 49 | empty |
| 4 | 127 | 0.56 | 0.83 | 26 | TRS |
| 5 | 167 | 0.54 | 0.79 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 1261 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
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 G0SG42
- Every structure of UniProt G0S9M2
- Elsewhere: RCSB PDB 5JQP · PDBe 5JQP · UniProt G0SG42 · UniProt G0S9M2
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