Research workbench
Structure of the pancreatic lipase-colipase complex
Analyse Structure of the pancreatic lipase-colipase complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1N8S
- Type
- protein
- Length
- 534 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.04
- Source
- Homo sapiens; Sus scrofa
- Molecule
- Triacylglycerol lipase, pancreatic; colipase II
- EC
- 3.1.1.3
- UniProt
- P16233, P02703
- Pockets
- 6 · best druggability 0.47
Structure
x-ray diffraction · resolution 3.04 · 2 distinct chains · 20% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Triacylglycerol lipase, pancreatic (EC 3.1.1.3) | protein | 449 | 22% helix, 30% strand | P16233 |
| C | colipase II | protein | 85 | 9% helix, 28% strand | P02703 |
Pockets
6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 233 | 0.47 | 0.74 | 25 | empty |
| 2 | 102 | 0.38 | 0.75 | 23 | empty |
| 3 | 76 | 0.37 | 0.77 | 16 | empty |
| 4 | 57 | 0.32 | 0.77 | 13 | empty |
| 5 | 63 | 0.29 | 0.74 | 15 | empty |
Interfaces
1 interface between chains.
- A–C · 535 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 11 disulfide (disulfide).
Compared structures
- 1N8S · Structure of the pancreatic lipase-colipase complex · 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 A against A, TM-score 0.99
- P02703 · AlphaFold monomer V2.0 prediction for colipase (P02703) · a predicted model of the same protein · chain C against A, TM-score 0.94
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 P16233
- Every structure of UniProt P02703
- Elsewhere: RCSB PDB 1N8S · PDBe 1N8S · UniProt P16233 · UniProt P02703
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