Research workbench
Golgi alpha-mannosidase II D341N acid-base catalyst mutant with bound mannose
Analyse Golgi alpha-mannosidase II D341N acid-base catalyst mutant with bound mannose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BUP
- Type
- protein
- Length
- 1,015 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-mannosidase 2
- EC
- 3.2.1.114
- UniProt
- Q24451
- Ligands
- NAG, MAN, ZN
- Pockets
- 13 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-mannosidase 2 (EC 3.2.1.114) | protein | 1015 | 24% helix, 30% strand | Q24451 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
- MAN · alpha-D-mannopyranose · sugar · chains A
- ZN · Zinc ion · metal · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 131 | 0.81 | 0.98 | 32 | empty |
| 2 | 161 | 0.78 | 0.95 | 29 | empty |
| 3 | 663 | 0.72 | 0.79 | 93 | empty |
| 4 | 286 | 0.63 | 0.80 | 31 | empty |
| 5 | 194 | 0.50 | 0.77 | 30 | MAN |
Modifications
Observed in the structure: 5 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 3BUP · Golgi alpha-mannosidase II D341N acid-base catalyst mutant with bound mannose · the same entry in another collection · chain A against A, TM-score 1.00
- Q24451 · AlphaFold monomer V2.0 prediction for alpha-mannosidase 2 (Q24451) · a predicted model of the same protein · 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 Q24451
- Elsewhere: RCSB PDB 3BUP · PDBe 3BUP · UniProt Q24451
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