Research workbench
The structural origins of interfacial activation in thermomyces (humicola) lanuginosa lipase
Analyse The structural origins of interfacial activation in thermomyces (humicola)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EIN
- Type
- protein
- Length
- 807 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipase
- EC
- 3.1.1.3
- UniProt
- O59952
- Ligands
- PLC
- Pockets
- 6 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Lipase (EC 3.1.1.3) | protein | 269 | 32% helix, 23% strand | O59952 |
Ligands and binding sites
- PLC · Diundecyl phosphatidyl choline · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1082 | 0.81 | 0.82 | 91 | PLC |
| 2 | 174 | 0.51 | 0.78 | 28 | empty |
| 3 | 177 | 0.49 | 0.77 | 29 | empty |
| 4 | 150 | 0.47 | 0.77 | 29 | empty |
| 5 | 62 | 0.27 | 0.73 | 16 | empty |
Interfaces
3 interfaces between chains.
- A–B · 492 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 484 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 475 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 9 disulfide (disulfide).
Compared structures
- 1EIN · The structural origins of interfacial activation in thermomyces (humicola) lanuginosa… · the same entry in another collection · chain B against B, TM-score 1.00
- O59952 · AlphaFold monomer V2.0 prediction for lipase (O59952) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 O59952
- Elsewhere: RCSB PDB 1EIN · PDBe 1EIN · UniProt O59952
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