MolNFT v1 · #1079 · protein
Crystal structure of bovine bile-salt activated lipase complexed with taurocholate
1AQL: “Crystal structure of bovine bile-salt activated lipase complexed with taurocholate”. X-ray diffraction, 2 ligands (TCH, NAG), 14 pockets (best druggability 0.72). MolNFT v1 #1079 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 1AQL
- Type
- protein
- Length
- 1,064 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bile-salt activated lipase
- EC
- 3.1.1.13
- UniProt
- P30122
- Ligands
- TCH, NAG
- Pockets
- 14 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Bile-salt activated lipase (EC 3.1.1.13) | protein | 532 | 37% helix, 16% strand | P30122 |
Ligands and binding sites
- TCH · Taurocholic acid · ligand · 4 copies · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 636 | 0.72 | 0.79 | 73 | empty |
| 2 | 530 | 0.71 | 0.80 | 58 | empty |
| 3 | 528 | 0.68 | 0.78 | 36 | TCH |
| 4 | 460 | 0.65 | 0.77 | 36 | TCH |
| 5 | 65 | 0.51 | 0.86 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 402 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
- 1AQL · Crystal structure of bovine bile-salt activated lipase complexed with taurocholate · the same entry in another collection · chain A against A, TM-score 1.00
- P30122 · AlphaFold monomer V2.0 prediction for bile salt-activated lipase (P30122) · 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 P30122
- Elsewhere: RCSB PDB 1AQL · PDBe 1AQL · UniProt P30122
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