Research workbench
Alpha-1,2-mannosidase from trichoderma reesei
Analyse Alpha-1,2-mannosidase from trichoderma reesei in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HCU
- Type
- protein
- Length
- 1,948 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-1,2-mannosidase
- EC
- 3.2.1.113
- UniProt
- Q9P8T8
- Ligands
- NAG, CA
- Pockets
- 8 · best druggability 0.75
Structure
x-ray diffraction · 4 distinct chains · 49% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-1,2-mannosidase (EC 3.2.1.113) | protein | 488 | 50% helix, 13% strand | Q9P8T8 |
| B | Alpha-1,2-mannosidase (EC 3.2.1.113) | protein | 489 | 49% helix, 13% strand | Q9P8T8 |
| C | Alpha-1,2-mannosidase (EC 3.2.1.113) | protein | 485 | 49% helix, 12% strand | Q9P8T8 |
| D | Alpha-1,2-mannosidase (EC 3.2.1.113) | protein | 486 | 48% helix, 13% strand | Q9P8T8 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 10 copies · chains A, B, C, D
- CA · Calcium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 936 | 0.75 | 0.78 | 108 | empty |
| 2 | 176 | 0.63 | 0.84 | 28 | CA |
| 3 | 186 | 0.62 | 0.83 | 27 | CA |
| 4 | 186 | 0.61 | 0.83 | 25 | CA |
| 5 | 171 | 0.59 | 0.82 | 26 | CA |
Interfaces
3 interfaces between chains.
- C–D · 218 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 151 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 67 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 glycan (N-glycosylation).
Compared structures
- 1HCU · alpha-1,2-mannosidase from Trichoderma reesei · 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 Q9P8T8
- Elsewhere: RCSB PDB 1HCU · PDBe 1HCU · UniProt Q9P8T8
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.