Research workbench
Structure of 1-17A4, a thermostable mutant of bacillus subtilis lipase obtained through directed evolution
Analyse Structure of 1-17A4, a thermostable mutant of bacillus subtilis lipase obtained… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3D2A
- Type
- protein
- Length
- 179 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipase
- EC
- 3.1.1.3
- UniProt
- P37957
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lipase (EC 3.1.1.3) | protein | 179 | 42% helix, 20% strand | P37957 |
Compared structures
- 3D2A · Structure of 1-17A4, a thermostable mutant of Bacillus subtilis lipase obtained through… · the same entry in another collection · chain A against A, TM-score 1.00
- P37957 · AlphaFold monomer V2.0 prediction for lipase esta (P37957) · 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 P37957
- Elsewhere: RCSB PDB 3D2A · PDBe 3D2A · UniProt P37957
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