Research workbench
Glucoamylase from saccharomycopsis fibuligera at atomic resolution
Analyse Glucoamylase from saccharomycopsis fibuligera at atomic resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FBA
- Type
- protein
- Length
- 492 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucoamylase GLU1
- EC
- 3.2.1.3
- UniProt
- P08017
- Pockets
- 3 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucoamylase GLU1 (EC 3.2.1.3) | protein | 492 | 51% helix, 8% strand | P08017 |
Ligands and binding sites
- 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
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 74 | 0.74 | 0.97 | 19 | empty |
| 2 | 130 | 0.55 | 0.82 | 25 | TRS |
| 3 | 84 | 0.45 | 0.80 | 20 | empty |
Compared structures
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 P08017
- Elsewhere: RCSB PDB 2FBA · PDBe 2FBA · UniProt P08017
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