Research workbench
Crystal structure analysis of the bacillus subtilis lipase crystallized at pH 4.5
Analyse Crystal structure analysis of the bacillus subtilis lipase crystallized at pH… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QXT
- Type
- protein
- Length
- 358 residues
- Chains
- 2
- 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 · 39% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Lipase (EC 3.1.1.3) | protein | 179 | 39% helix, 20% strand | P37957 |
Compared structures
- 2QXT · Crystal Structure Analysis of the Bacillus subtilis lipase crystallized at pH 4.5 · 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 2QXT · PDBe 2QXT · UniProt P37957
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