Research workbench
Mutant (D193N) maltotetraose-forming exo-amylase in complex with maltotetraose
Analyse Mutant (D193N) maltotetraose-forming exo-amylase in complex with maltotetraose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QI3
- Type
- protein
- Length
- 418 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (exo-maltotetraohydrolase)
- EC
- 3.2.1.60
- UniProt
- P13507
- Ligands
- GLC, CA
- Pockets
- 2 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (exo-maltotetraohydrolase) (EC 3.2.1.60) | protein | 418 | 35% helix, 18% strand | P13507 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 4 copies · chains A
- CA · Calcium ion · metal · 2 copies · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 283 | 0.58 | 0.78 | 33 | GLC |
| 2 | 134 | 0.54 | 0.81 | 24 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1QI3 · Mutant (D193N) maltotetraose-forming exo-amylase in complex with maltotetraose · the same entry in another collection · chain A against A, TM-score 1.00
- P13507 · AlphaFold monomer V2.0 prediction for glucan 1,4-alpha- maltotetraohydrolase (P13507) · 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 P13507
- Elsewhere: RCSB PDB 1QI3 · PDBe 1QI3 · UniProt P13507
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