Research workbench
The roles of GLU186 and GLU380 in the catalytic reaction of soybean beta-amylase
Analyse The roles of GLU186 and GLU380 in the catalytic reaction of soybean beta-amylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1V3H
- Type
- protein
- Length
- 491 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P10538
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 491 | — | P10538 |
Compared structures
- 1V3H · The roles of Glu186 and Glu380 in the catalytic reaction of soybean beta-amylase · the same entry in another collection · chain A against A, TM-score 1.00
- P10538 · AlphaFold monomer V2.0 prediction for beta-amylase (P10538) · 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 P10538
- Elsewhere: RCSB PDB 1V3H · PDBe 1V3H · UniProt P10538
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