Research workbench
Acarbose complex of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.93A
Analyse Acarbose complex of chimaeric amylase from B. amyloliquefaciens and B.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1E3Z
- Type
- protein
- Length
- 483 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00692, P06278
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 483 | — | P00692, P06278 |
Compared structures
- 1E3Z · Acarbose complex of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at… · the same entry in another collection · chain A against A, TM-score 1.00
- P00692 · AlphaFold monomer V2.0 prediction for alpha-amylase (P00692) · a predicted model of the same protein · chain A against A, TM-score 1.00
- P06278 · AlphaFold monomer V2.0 prediction for alpha-amylase (P06278) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P00692
- Every structure of UniProt P06278
- Elsewhere: RCSB PDB 1E3Z · PDBe 1E3Z · UniProt P00692 · UniProt P06278
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