MolNFT v1 · #9225 · protein
Horse pancreatic lipase. the crystal structure at 2.3 ångströms resolution
1HPL: “Horse pancreatic lipase. the crystal structure at 2.3 ångströms resolution”. X-ray diffraction, 1 ligand (CA), 8 pockets (best druggability 0.66). MolNFT v1 #9225 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1HPL
- Type
- protein
- Length
- 898 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipase
- EC
- 3.1.1.3
- UniProt
- P29183
- Ligands
- CA
- Pockets
- 8 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Lipase (EC 3.1.1.3) | protein | 449 | 23% helix, 31% strand | P29183 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 372 | 0.66 | 0.80 | 37 | empty |
| 2 | 159 | 0.64 | 0.86 | 21 | empty |
| 3 | 379 | 0.62 | 0.77 | 45 | empty |
| 4 | 214 | 0.57 | 0.80 | 26 | empty |
| 5 | 317 | 0.54 | 0.75 | 41 | empty |
Interfaces
1 interface between chains.
- A–B · 1011 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 disulfide (disulfide).
Compared structures
- 1HPL · Horse pancreatic lipase. the crystal structure at 2.3 ångströms resolution · the same entry in another collection · chain A against A, TM-score 1.00
- P29183 · AlphaFold monomer V2.0 prediction for pancreatic triacylglycerol lipase (P29183) · 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 P29183
- Elsewhere: RCSB PDB 1HPL · PDBe 1HPL · UniProt P29183
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