Research workbench
Crystal structure of sarin surrogate NIMP inhibited recombinant human bile salt activated lipase
Analyse Crystal structure of sarin surrogate NIMP inhibited recombinant human bile salt… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6H18
- Type
- protein
- Length
- 523 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.85
- Source
- Homo sapiens
- Molecule
- Bile salt-activated lipase
- EC
- 3.1.1.13, 3.1.1.3
- UniProt
- P19835
- Ligands
- ZN
- Pockets
- 4 · best druggability 0.69
Structure
x-ray diffraction · resolution 1.85 · 1 distinct chain · 37% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bile salt-activated lipase (EC 3.1.1.13, 3.1.1.3) | protein | 523 | 37% helix, 17% strand | P19835 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 590 | 0.69 | 0.78 | 60 | ZN, ACT |
| 2 | 489 | 0.63 | 0.75 | 37 | ZN, ACT |
| 3 | 59 | 0.51 | 0.86 | 20 | empty |
| 4 | 70 | 0.34 | 0.76 | 16 | empty |
Modifications
Observed in the structure: 2 disulfide, 1 modified (disulfide, nonstandard).
Compared structures
- 6H18 · Crystal structure of sarin surrogate nimp inhibited recombinant human bile salt activated… · the same entry in another collection · chain A against A, TM-score 1.00
- P19835 · AlphaFold monomer V2.0 prediction for bile salt-activated lipase (P19835) · 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 P19835
- Elsewhere: RCSB PDB 6H18 · PDBe 6H18 · UniProt P19835
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