MolNFT v1 · #58248 · protein
Crystal structure of isomaltase in complex with maltose
3AXI · Oligo-1,6-glucosidase IMA1: “Crystal structure of isomaltase in complex with maltose”. X-ray diffraction, 2 ligands (GLC, CA), 6 pockets (best druggability 0.79). MolNFT v1 #58248 on GenesisL1: 3D structure, binding sites and…
- PDB
- 3AXI
- Type
- protein
- Length
- 586 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Oligo-1,6-glucosidase IMA1
- EC
- 3.2.1.10
- UniProt
- P53051
- Ligands
- GLC, CA
- Pockets
- 6 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Oligo-1,6-glucosidase IMA1 (EC 3.2.1.10) | protein | 586 | 33% helix, 19% strand | P53051 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 396 | 0.79 | 0.88 | 43 | GLC |
| 2 | 197 | 0.57 | 0.80 | 25 | empty |
| 3 | 73 | 0.49 | 0.84 | 18 | empty |
| 4 | 61 | 0.34 | 0.77 | 19 | empty |
| 5 | 93 | 0.31 | 0.73 | 18 | 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 P53051
- Elsewhere: RCSB PDB 3AXI · PDBe 3AXI · UniProt P53051
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