Research workbench
Crystal structure of glva from bacillus subtilis, a metal-requiring, NAD-dependent 6-phospho-alpha-glucosidase
Analyse Crystal structure of glva from bacillus subtilis, a metal-requiring… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1U8X
- Type
- protein
- Length
- 436 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maltose-6'-phosphate glucosidase
- EC
- 3.2.1.122
- UniProt
- P54716
- Ligands
- NAD, G6P, MN
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Maltose-6'-phosphate glucosidase (EC 3.2.1.122) | protein | 436 | 47% helix, 17% strand | P54716 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · chains X
- G6P · 6-O-phosphono-alpha-D-glucopyranose · sugar · chains X
- MN · Manganese (II) ion · metal · chains X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 743 | 0.76 | 0.81 | 77 | G6P, MN, NAD |
| 2 | 51 | 0.65 | 0.95 | 15 | empty |
| 3 | 138 | 0.47 | 0.77 | 20 | empty |
| 4 | 64 | 0.43 | 0.82 | 12 | empty |
Modifications
Observed in the structure: 16 modified (engineered).
Compared structures
- 1U8X · Crystal structure of glva from bacillus subtilis, a metal-requiring, NAD-dependent… · the same entry in another collection · chain X against X, TM-score 1.00
- P54716 · AlphaFold monomer V2.0 prediction for maltose-6'-phosphate glucosidase (P54716) · a predicted model of the same protein · chain X against A, TM-score 0.99
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 P54716
- Elsewhere: RCSB PDB 1U8X · PDBe 1U8X · UniProt P54716
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