Research workbench
Structure of human pancreatic lipase related protein 2 mutant N336Q
Analyse Structure of human pancreatic lipase related protein 2 mutant N336Q in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PVS
- Type
- protein
- Length
- 880 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pancreatic lipase-related protein 2
- EC
- 3.1.1.3
- UniProt
- P54317
- Ligands
- CA, SO4
- Pockets
- 5 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 22% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pancreatic lipase-related protein 2 (EC 3.1.1.3) | protein | 435 | 22% helix, 29% strand | P54317 |
| B | Pancreatic lipase-related protein 2 (EC 3.1.1.3) | protein | 445 | 22% helix, 30% strand | P54317 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1029 | 0.79 | 0.81 | 109 | SO4 |
| 2 | 95 | 0.40 | 0.77 | 18 | empty |
| 3 | 71 | 0.34 | 0.76 | 17 | empty |
| 4 | 70 | 0.33 | 0.76 | 14 | empty |
| 5 | 64 | 0.33 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1055 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 disulfide (disulfide).
Compared structures
- 2PVS · Structure of human pancreatic lipase related protein 2 mutant N336Q · the same entry in another collection · chain B against B, TM-score 1.00
- P54317 · AlphaFold monomer V2.0 prediction for pancreatic lipase-related protein 2 (P54317) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 P54317
- Elsewhere: RCSB PDB 2PVS · PDBe 2PVS · UniProt P54317
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