Research workbench
Solution strucuture of the CBM25-1 of BETA/ALPHA-amylase from paenibacillus polymyxa
Analyse Solution strucuture of the CBM25-1 of BETA/ALPHA-amylase from paenibacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LAA
- Type
- protein
- Length
- 104 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BETA/ALPHA-amylase
- EC
- 3.2.1.2, 3.2.1.1
- UniProt
- P21543
Structure
solution nmr · 1 distinct chain · 0% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | BETA/ALPHA-amylase (EC 3.2.1.2, 3.2.1.1) | protein | 104 | 0% helix, 44% strand | P21543 |
Compared structures
- 2LAA · Solution Strucuture of the CBM25-1 of beta/alpha-amylase from Paenibacillus polymyxa · the same entry in another collection · chain A against A, TM-score 1.00
- P21543 · AlphaFold monomer V2.0 prediction for BETA/ALPHA-amylase (P21543) · a predicted model of the same protein · chain A against A, TM-score 0.86
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 P21543
- Elsewhere: RCSB PDB 2LAA · PDBe 2LAA · UniProt P21543
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