Research workbench
Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography
Analyse Interfacial activation of the lipase-procolipase complex by mixed micelles… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LPA
- Type
- protein
- Length
- 534 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Colipase; Lipase
- EC
- 3.1.1.3
- UniProt
- P02703, P16233
- Ligands
- BNG, PLC, CA
- Pockets
- 5 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 21% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Colipase | protein | 85 | 4% helix, 29% strand | P02703 |
| B | Lipase (EC 3.1.1.3) | protein | 449 | 24% helix, 30% strand | P16233 |
Ligands and binding sites
- BNG · nonyl beta-D-glucopyranoside · ligand · chains B
- PLC · Diundecyl phosphatidyl choline · ligand · chains B
- CA · Calcium ion · metal · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 380 | 0.57 | 0.75 | 57 | empty |
| 2 | 135 | 0.51 | 0.79 | 19 | PLC |
| 3 | 90 | 0.38 | 0.76 | 17 | empty |
| 4 | 72 | 0.31 | 0.74 | 19 | empty |
| 5 | 70 | 0.29 | 0.72 | 10 | empty |
Interfaces
1 interface between chains.
- A–B · 825 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 11 disulfide (disulfide).
Compared structures
- 1LPA · Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by… · the same entry in another collection · chain A against A, TM-score 1.00
- P16233 · AlphaFold monomer V2.0 prediction for pancreatic triacylglycerol lipase (P16233) · a predicted model of the same protein · chain B against A, TM-score 0.95
- P02703 · AlphaFold monomer V2.0 prediction for colipase (P02703) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 P02703
- Every structure of UniProt P16233
- Elsewhere: RCSB PDB 1LPA · PDBe 1LPA · UniProt P02703 · UniProt P16233
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