Research workbench
Structure of the catalytic domain of human bile salt activated lipase
Analyse Structure of the catalytic domain of human bile salt activated lipase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1F6W
- Type
- protein
- Length
- 533 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P19835
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 533 | — | P19835 |
Compared structures
- 1F6W · Structure of the catalytic domain of human bile salt activated lipase · the same entry in another collection · chain A against A, TM-score 1.00
- P19835 · AlphaFold monomer V2.0 prediction for bile salt-activated lipase (P19835) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P19835
- Elsewhere: RCSB PDB 1F6W · PDBe 1F6W · UniProt P19835
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