Research workbench
Structure of bacillus halmapalus alpha-amylase, crystallized with the substrate analogue acarbose and maltose
Analyse Structure of bacillus halmapalus alpha-amylase, crystallized with the substrate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GJP
- Type
- protein
- Length
- 481 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P19571
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 481 | — | P19571 |
Compared structures
- 2GJP · Structure of Bacillus halmapalus alpha-amylase, crystallized with the substrate analogue… · the same entry in another collection · chain A against A, TM-score 1.00
- P19571 · AlphaFold monomer V2.0 prediction for glucan 1,4-alpha- maltohexaosidase (P19571) · 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 P19571
- Elsewhere: RCSB PDB 2GJP · PDBe 2GJP · UniProt P19571
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