MolNFT v1 · #96395 · protein
Structural analysis and insights into glycon specificity of the rice GH1 OS7BGLU26 beta-D-mannosidase
4JIE · Beta-MANNOSIDASE/BETA-glucosidase: “Structural analysis and insights into glycon specificity of the rice GH1 OS7BGLU26 beta-D-mannosidase”. X-ray diffraction, 1 ligand (BMA), 2 pockets (best druggability 0.76). MolNFT v1 #96395 on…
- PDB
- 4JIE
- Type
- protein
- Length
- 484 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-MANNOSIDASE/BETA-glucosidase
- EC
- 3.2.1.25
- UniProt
- B5ABY0
- Ligands
- BMA
- Pockets
- 2 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-MANNOSIDASE/BETA-glucosidase (EC 3.2.1.25) | protein | 484 | 44% helix, 16% strand | B5ABY0 |
Ligands and binding sites
- BMA · beta-D-mannopyranose · sugar · chains A
- GOL · Glycerol · additive · 6 copies · chains A
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 352 | 0.76 | 0.86 | 38 | GOL, EPE, BMA |
| 2 | 61 | 0.28 | 0.74 | 14 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 4JIE · Structural analysis and insights into glycon specificity of the rice GH1 Os7BGlu26… · 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 B5ABY0
- Elsewhere: RCSB PDB 4JIE · PDBe 4JIE · UniProt B5ABY0
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