Research workbench
Crystal structure of native recombinant human bile salt activated lipase
Analyse Crystal structure of native recombinant 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
- 6H0T
- Type
- protein
- Length
- 514 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bile salt-activated lipase
- EC
- 3.1.1.13, 3.1.1.3
- UniProt
- P19835
- Ligands
- ZN
- Pockets
- 6 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bile salt-activated lipase (EC 3.1.1.13, 3.1.1.3) | protein | 514 | 39% helix, 17% strand | P19835 |
Ligands and binding sites
- ZN · Zinc ion · metal · 8 copies · chains A
- ACT · Acetate ion · additive · 4 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 473 | 0.70 | 0.80 | 44 | empty |
| 2 | 512 | 0.65 | 0.76 | 36 | empty |
| 3 | 104 | 0.49 | 0.81 | 26 | GOL |
| 4 | 116 | 0.39 | 0.75 | 27 | empty |
| 5 | 73 | 0.35 | 0.76 | 14 | ZN, ACT |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6H0T · Crystal structure of native recombinant 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 0.99
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 6H0T · PDBe 6H0T · UniProt P19835
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